2WZV - JenaLib

Asymmetric Unit (8, 8)

No.	Name	Evidence	Residues	Description
1	AC1	SOFTWARE	ARG A:25 , ARG A:26 , ALA A:27 , ARG A:29 , PHE A:108 , TYR A:137 , PRO A:179 , GLN A:180 , ALA A:181 , LEU A:182 , MSE A:203 , ILE A:221 , ARG A:223 , HOH A:2015 , HOH A:2109 , HOH A:2171 , HOH A:2172 , HOH A:2173 , HOH A:2174 , PRO B:52 , SER B:53 , ASN B:54 , ASN B:56 , ASP B:158 , ILE B:161 , PO4 B:1235	BINDING SITE FOR RESIDUE FMN A 801
2	AC2	SOFTWARE	PRO A:52 , SER A:53 , ASN A:54 , ASP A:158 , ILE A:161 , PO4 A:1235 , ARG B:25 , ARG B:26 , ALA B:27 , ARG B:29 , PHE B:108 , TYR B:137 , PRO B:179 , GLN B:180 , ALA B:181 , LEU B:182 , ILE B:221 , ARG B:223 , HOH B:2094 , HOH B:2100 , HOH B:2173 , HOH B:2174	BINDING SITE FOR RESIDUE FMN B 801
3	AC3	SOFTWARE	SER A:55 , HOH A:2175 , HOH A:2176 , HOH A:2177 , HOH A:2178 , PHE B:108 , FMN B:801	BINDING SITE FOR RESIDUE PO4 A1235
4	AC4	SOFTWARE	PHE A:108 , FMN A:801 , SER B:55 , HOH B:2175 , HOH B:2176 , HOH B:2177	BINDING SITE FOR RESIDUE PO4 B1235
5	AC5	SOFTWARE	ARG B:32 , PRO B:33 , ASP B:34 , HIS B:173 , HOH B:2178 , HOH B:2179	BINDING SITE FOR RESIDUE PO4 B1236
6	AC6	SOFTWARE	GLY A:24 , ARG A:26 , THR A:171 , ILE A:175 , HOH A:2013 , HOH A:2179 , HOH A:2180	BINDING SITE FOR RESIDUE GOL A1236
7	AC7	SOFTWARE	ARG A:234 , ALA B:68 , ARG B:72	BINDING SITE FOR RESIDUE GOL A1237
8	AC8	SOFTWARE	PRO A:91 , THR A:151 , GLU A:152 , ARG B:93 , GLU B:152 , ALA B:153 , HOH B:2074 , HOH B:2110	BINDING SITE FOR RESIDUE GOL B1237

SS Bonds (0, 0)

Cis Peptide Bonds (0, 0)

Sequence-Structure Mapping

SAPs(SNPs)/Variants (0, 0)

PROSITE Motifs (0, 0)

Exons (0, 0)

Sequences/Alignments

Asymmetric/Biological Unit

Reformat:	Number of residues per line = ('0' or empty: single-line sequence representation)
	Number of residues per labelling interval =
	UniProt sequence: complete aligned part

Show mapping:	SCOP domains	CATH domains	Pfam domains	Secondary structure (by author)
	SAPs(SNPs)	PROSITE motifs	Exons
	(details for a mapped element are shown in a popup box when the mouse pointer rests over it)

Chain A from PDB  Type:PROTEIN  Length:222
 aligned with NFNB_MYCS2 | A0R6D0 from UniProtKB/Swiss-Prot  Length:234

    Alignment length:222
                                    22        32        42        52        62        72        82        92       102       112       122       132       142       152       162       172       182       192       202       212       222       232  
           NFNB_MYCS2    13 DLAQAAERLIKGRRAVRAFRPDEVPEETMRAVFELAGHAPSNSNTQPWHVEVVSGAARDRLAEALVTAHAEERVTVDFPYREGLFQGVLQERRADFGSRLYAALGIARDQTDLLQGYNTESLRFYGAPHVAMLFAPNNTEARIAGDMGIYAQTLMLAMTAHGIASCPQALLSFYADTVRAELGVENRKLLMGISFGYADDTAAVNGVRIPRAGLSETTRFSR 234
               SCOP domains ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ SCOP domains
               CATH domains ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ CATH domains
               Pfam domains ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ Pfam domains
         Sec.struct. author hhhhhhhhhhhhh...........hhhhhhhhhhhhh...hhhhh...eeeeehhhhhhhhhhhhhhhhhh..............hhhhhhhhhhhhhhhhhhhh....hhhhhhhhhhhhhhhhhh.eeeeeeee...hhhhhhhhhhhhhhhhhhhhhh..eeeeehhhhhhhhhhhhhhh...eeeeeeeeee.....hhhhhh.....hhhhheeee. Sec.struct. author
                 SAPs(SNPs) ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ SAPs(SNPs)
                    PROSITE ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ PROSITE
                 Transcript ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ Transcript
                 2wzv A  13 DLAQAAERLIKGRRAVRAFRPDEVPEETmRAVFELAGHAPSNSNTQPWHVEVVSGAARDRLAEALVTAHAEERVTVDFPYREGLFQGVLQERRADFGSRLYAALGIARDQTDLLQGYNTESLRFYGAPHVAmLFAPNNTEARIAGDmGIYAQTLmLAmTAHGIASCPQALLSFYADTVRAELGVENRKLLmGISFGYADDTAAVNGVRIPRAGLSETTRFSR 234
                                    22        32        42        52        62        72        82        92       102       112       122       132       142 |     152      |162    |  172       182       192       202|      212       222       232  
                                                       41-MSE                                                                                                144-MSE        159-MSE 167-MSE                             203-MSE                           
                                                                                                                                                                                       170-MSE

Chain B from PDB  Type:PROTEIN  Length:223
 aligned with NFNB_MYCS2 | A0R6D0 from UniProtKB/Swiss-Prot  Length:234

    Alignment length:223
                                    21        31        41        51        61        71        81        91       101       111       121       131       141       151       161       171       181       191       201       211       221       231   
           NFNB_MYCS2    12 VDLAQAAERLIKGRRAVRAFRPDEVPEETMRAVFELAGHAPSNSNTQPWHVEVVSGAARDRLAEALVTAHAEERVTVDFPYREGLFQGVLQERRADFGSRLYAALGIARDQTDLLQGYNTESLRFYGAPHVAMLFAPNNTEARIAGDMGIYAQTLMLAMTAHGIASCPQALLSFYADTVRAELGVENRKLLMGISFGYADDTAAVNGVRIPRAGLSETTRFSR 234
               SCOP domains ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SCOP domains
               CATH domains ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- CATH domains
               Pfam domains ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author .hhhhhhhhhhhhh...........hhhhhhhhhhhhh...hhhhh...eeeeehhhhhhhhhhhhhhhhhh...............hhhhhhhhhhhhhhhhhhh....hhhhhhhhhhhhhhhhhh.eeeeeee....hhhhhhhhhhhhhhhhhhhhhh..eeeeehhhhhhhhhhhhhhh....eeeeeeeee.....hhhhhh.....hhhhheeee. Sec.struct. author
                 SAPs(SNPs) ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- PROSITE
                 Transcript ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Transcript
                 2wzv B  12 VDLAQAAERLIKGRRAVRAFRPDEVPEETmRAVFELAGHAPSNSNTQPWHVEVVSGAARDRLAEALVTAHAEERVTVDFPYREGLFQGVLQERRADFGSRLYAALGIARDQTDLLQGYNTESLRFYGAPHVAmLFAPNNTEARIAGDmGIYAQTLmLAmTAHGIASCPQALLSFYADTVRAELGVENRKLLmGISFGYADDTAAVNGVRIPRAGLSETTRFSR 234
                                    21        31        41        51        61        71        81        91       101       111       121       131       141  |    151       161     | 171       181       191       201 |     211       221       231   
                                                        41-MSE                                                                                                144-MSE        159-MSE 167-MSE                             203-MSE                           
                                                                                                                                                                                        170-MSE

Legend:		→ Mismatch	(orange background)
	-	→ Gap	(green background, '-', border residues have a numbering label)
		→ Modified Residue	(blue background, lower-case, 'x' indicates undefined single-letter code, labelled with number + name)
	x	→ Chemical Group	(purple background, 'x', labelled with number + name, e.g. ACE or NH2)
	extra numbering lines below/above indicate numbering irregularities and modified residue names etc., number ends below/above '\|'

Classification and Annotation

SCOP Domains (0, 0)

CATH Domains (0, 0)

Pfam Domains (0, 0)

Gene Ontology (8, 8)

Asymmetric/Biological Unit(hide GO term definitions)

Chain A,B (NFNB_MYCS2 | A0R6D0)

molecular function
	GO:0010181	FMN binding	Interacting selectively and non-covalently with flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
	GO:0050661	NADP binding	Interacting selectively and non-covalently with nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.
	GO:0042802	identical protein binding	Interacting selectively and non-covalently with an identical protein or proteins.
	GO:0000166	nucleotide binding	Interacting selectively and non-covalently with a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.
	GO:0016491	oxidoreductase activity	Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
	GO:0042803	protein homodimerization activity	Interacting selectively and non-covalently with an identical protein to form a homodimer.
biological process
	GO:2001039	negative regulation of cellular response to drug	Any process that stops, prevents or reduces the frequency, rate or extent of cellular response to drug.
	GO:0055114	oxidation-reduction process	A metabolic process that results in the removal or addition of one or more electrons to or from a substance, with or without the concomitant removal or addition of a proton or protons.

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	2wzv
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Description

Compounds

Structural Features

Chains, Units

Ligands, Modified Residues, Ions (4, 20)

Sites (8, 8)