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(-) Description

Title :  STRUCTURE OF THE ENOYL-ACP REDUCTASE OF MYCOBACTERIUM TUBERCULOSIS INHA, INHIBITED WITH THE ACTIVE METABOLITE OF ISONIAZID
 
Authors :  A. Chollet, S. Julien, L. Mourey, L. Maveyraud
Date :  17 Jun 14  (Deposition) - 29 Apr 15  (Release) - 17 Jun 15  (Revision)
Method :  X-RAY DIFFRACTION
Resolution :  1.40
Chains :  Asym. Unit :  A
Biol. Unit 1:  A  (4x)
Keywords :  Isoniazid, Oxidoreductase (Keyword Search: [Gene Ontology, PubMed, Web (Google)] )
 
Reference :  A. Chollet, L. Mourey, C. Lherbet, A. Delbot, S. Julien, M. Baltas, J. Bernadou, G. Pratviel, L. Maveyraud, V. Bernardes-Genisson
Crystal Structure Of The Enoyl-Acp Reductase Of Mycobacterium Tuberculosis (Inha) In The Apo-Form And In Complex With The Active Metabolite Of Isoniazid Pre-Formed By A Biomimetic Approach.
J. Struct. Biol. V. 190 328 2015
PubMed-ID: 25891098  |  Reference-DOI: 10.1016/J.JSB.2015.04.008

(-) Compounds

Molecule 1 - ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH]
    Chains: A
    EC Number: 1.3.1.9
    Engineered: YES
    Expression System: ESCHERICHIA COLI
    Expression System Strain: BL21(DE3)
    Expression System Taxid: 469008
    Gene: INHA
    Organism Scientific: MYCOBACTERIUM TUBERCULOSIS
    Organism Taxid: 1773

 Structural Features

(-) Chains, Units

  1
Asymmetric Unit : A
Biological Unit 1 (4x): A

Summary Information (see also Sequences/Alignments below)

(-) Ligands, Modified Residues, Ions  (5, 10)

Asymmetric Unit (5, 10)
No.NameCountTypeFull Name
1DMS4Ligand/IonDIMETHYL SULFOXIDE
2EPE2Ligand/Ion4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
3NA2Ligand/IonSODIUM ION
4NAD1Ligand/IonNICOTINAMIDE-ADENINE-DINUCLEOTIDE
5ZID1Ligand/IonISONICOTINIC-ACETYL-NICOTINAMIDE-ADENINE DINUCLEOTIDE
Biological Unit 1 (4, 32)
No.NameCountTypeFull Name
1DMS16Ligand/IonDIMETHYL SULFOXIDE
2EPE8Ligand/Ion4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
3NA-1Ligand/IonSODIUM ION
4NAD4Ligand/IonNICOTINAMIDE-ADENINE-DINUCLEOTIDE
5ZID4Ligand/IonISONICOTINIC-ACETYL-NICOTINAMIDE-ADENINE DINUCLEOTIDE

(-) Sites  (10, 10)

Asymmetric Unit (10, 10)
No.NameEvidenceResiduesDescription
01AC1SOFTWAREGLY A:14 , ILE A:15 , ILE A:16 , SER A:20 , ILE A:21 , PHE A:41 , LEU A:63 , ASP A:64 , VAL A:65 , SER A:94 , ILE A:95 , GLY A:96 , MET A:147 , ASP A:148 , LYS A:165 , ALA A:191 , GLY A:192 , PRO A:193 , ILE A:194 , THR A:196 , ZID A:302 , HOH A:479 , HOH A:490 , HOH A:502 , HOH A:504 , HOH A:528 , HOH A:543 , HOH A:553 , HOH A:576 , HOH A:619 , HOH A:620binding site for residue NAD A 301
02AC2SOFTWAREGLY A:14 , ILE A:15 , ILE A:16 , SER A:20 , ILE A:21 , PHE A:41 , LEU A:63 , ASP A:64 , VAL A:65 , SER A:94 , ILE A:95 , GLY A:96 , ILE A:122 , MET A:147 , ASP A:148 , PHE A:149 , TYR A:158 , LYS A:165 , ALA A:191 , GLY A:192 , PRO A:193 , ILE A:194 , THR A:196 , TRP A:222 , NAD A:301 , HOH A:479 , HOH A:502 , HOH A:504 , HOH A:528 , HOH A:529 , HOH A:543 , HOH A:553 , HOH A:576 , HOH A:617 , HOH A:619 , HOH A:620 , HOH A:664binding site for residue ZID A 302
03AC3SOFTWAREASP A:42 , LEU A:44 , ARG A:45 , GLU A:62 , HIS A:70 , HOH A:501 , HOH A:511 , HOH A:532binding site for residue EPE A 303
04AC4SOFTWARESER A:19 , HIS A:24 , ILE A:194 , ARG A:195 , THR A:196 , LYS A:233 , ASP A:234 , ALA A:235 , HOH A:407 , HOH A:411binding site for residue EPE A 304
05AC5SOFTWAREILE A:228 , GLY A:229 , HOH A:571binding site for residue DMS A 305
06AC6SOFTWAREGLY A:141 , GLY A:183 , ARG A:185 , ILE A:228 , PRO A:251binding site for residue DMS A 306
07AC7SOFTWAREPHE A:109 , LYS A:132 , PRO A:136 , TYR A:182 , HOH A:460 , HOH A:648 , HOH A:660binding site for residue DMS A 307
08AC8SOFTWAREGLU A:68 , ASP A:110 , LYS A:132 , HOH A:454binding site for residue DMS A 308
09AC9SOFTWAREASP A:223 , GLN A:224 , ALA A:226 , HOH A:612 , HOH A:627 , HOH A:666binding site for residue NA A 309
10AD1SOFTWAREGLY A:141 , ASP A:248 , HOH A:470binding site for residue NA A 310

(-) SS Bonds  (0, 0)

(no "SS Bond" information available for 4TRO)

(-) Cis Peptide Bonds  (0, 0)

(no "Cis Peptide Bond" information available for 4TRO)

 Sequence-Structure Mapping

(-) SAPs(SNPs)/Variants  (0, 0)

(no "SAP(SNP)/Variant" information available for 4TRO)

(-) PROSITE Motifs  (0, 0)

(no "PROSITE Motif" information available for 4TRO)

(-) Exons   (0, 0)

(no "Exon" information available for 4TRO)

(-) Sequences/Alignments

Asymmetric 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:268
                                                                                                                                                                                                                                                                                                            
               SCOP domains ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SCOP domains
               CATH domains ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- CATH domains
               Pfam domains ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author .......eeeee......hhhhhhhhhhhhh..eeeeee..hhhhhhhhhh.......eee....hhhhhhhhhhhhhhhhh....eeeeee.....hhhhh...hhhhhhhhhhhhhhhhhhhhhhhhhhhhh..eeeeeeeeeee.........hhhhhhhhhhhhhhhhhhhhhhhh...eeeeeee....hhhhhhhhh...hhhhhhhhhhhhhhhhhhh........hhhhhhhhhhhhh........eeeee..hhhhh.. Sec.struct. author
                 SAPs(SNPs) ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- PROSITE
                 Transcript ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Transcript
                 4tro A   2 TGLLDGKRILVSGIITDSSIAFHIARVAQEQGAQLVLTGFDRLRLIQRITDRLPAKAPLLELDVQNEEHLASLAGRVTEAIGAGNKLDGVVHSIGFMPQTGMGINPFFDAPYADVSKGIHISAYSYASMAKALLPIMNPGGSIVGMDFDPSRAMPAYNWMTVAKSALESVNRFVAREAGKYGVRSNLVAAGPIRTLAMSAIVGGALGEEAGAQIQLLEEGWDQRAPIGWNMKDATPVAKTVCALLSDWLPATTGDIIYADGGAHTQLL 269
                                    11        21        31        41        51        61        71        81        91       101       111       121       131       141       151       161       171       181       191       201       211       221       231       241       251       261
   Legend:   → Mismatch (orange background)
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  extra numbering lines below/above indicate numbering irregularities and modified residue names etc., number ends below/above '|'

 Classification and Annotation

(-) SCOP Domains  (0, 0)

(no "SCOP Domain" information available for 4TRO)

(-) CATH Domains  (0, 0)

(no "CATH Domain" information available for 4TRO)

(-) Pfam Domains  (0, 0)

(no "Pfam Domain" information available for 4TRO)

(-) Gene Ontology  (13, 17)

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  4tro
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  INHA_MYCTU | P9WGR1
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  M9TGV3_MYCTX | M9TGV3
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  1.3.1.9
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 Related Entries

(-) Entries Sharing at Least One Protein Chain (UniProt ID)

UniProtKB/Swiss-Prot
        INHA_MYCTU | P9WGR1: 1bvr 1eny 1enz 1p44 1p45 1zid 2aq8 2aqh 2aqi 2aqk 2b35 2b36 2b37 2h9i 2idz 2ie0 2ieb 2ied 2nsd 2ntj 2nv6 2pr2 2x22 2x23 3fne 3fnf 3fng 3fnh 3oew 3oey 3of2 4bge 4bgi 4bii 4bqp 4bqr 4cod 4d0r 4d0s 4dqu 4dre 4dti 4ohu 4oim 4oxk 4oxn 4oxy 4oyr 4qxm 4r9r 4r9s 4trj 4trm 4trn 4tzk 4tzt 4u0j 4u0k 4uvd 4uve 4uvg 4uvh 4uvi 5coq 5cp8 5cpb 5cpf 5g0s 5g0t 5g0u 5g0v 5g0w 5jfo 5mtp 5mtq 5mtr 5ugs 5ugt 5ugu
        M9TGV3_MYCTX | M9TGV3: 4uvd 4uve 4uvg 4uvh 4uvi 5coq 5cp8 5cpb 5g0w

(-) Related Entries Specified in the PDB File

4trm 4TRM CONTAINS THE NATIVE APO STRUCTURE
4trn 4TRN CONTAINS THE SAME PROTEIN COMPLEXED WITH NADH