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(-) Description

Title :  PROPOSED AMINO ACID SEQUENCE AND THE 1.63 ANGSTROM X-RAY CRYSTAL STRUCTURE OF A PLANT CYSTEINE PROTEASE ERVATAMIN B: INSIGHT INTO THE STRUCTURAL BASIS OF ITS STABILITY AND SUBSTRATE SPECIFICITY.
 
Authors :  C. Chakrabarti, S. Biswas, J. K. Dattagupta
Date :  02 May 02  (Deposition) - 06 May 03  (Release) - 13 Jul 11  (Revision)
Method :  X-RAY DIFFRACTION
Resolution :  1.63
Chains :  Asym./Biol. Unit :  A
Keywords :  Cysteine Protease, Alpha-Beta Protein, Catalytic Dyad, L-Domain, R- Domain. , Hydrolase (Keyword Search: [Gene Ontology, PubMed, Web (Google)] )
 
Reference :  S. Biswas, C. Chakrabarti, S Kundu, M. V. Jagannadham, J. K. Dattagupta
Proposed Amino Acid Sequence And The 1. 63 A X-Ray Crystal Structure Of A Plant Cysteine Protease, Ervatamin B: Some Insights Into The Structural Basis Of Its Stability And Substrate Specificity
Proteins V. 51 489 2003
PubMed-ID: 12784208  |  Reference-DOI: 10.1002/PROT.10319

(-) Compounds

Molecule 1 - ERVATAMIN B
    Chains: A
    Organism Scientific: TABERNAEMONTANA DIVARICATA
    Organism Taxid: 52861

 Structural Features

(-) Chains, Units

  1
Asymmetric/Biological Unit : A

Summary Information (see also Sequences/Alignments below)

(-) Ligands, Modified Residues, Ions  (1, 1)

Asymmetric/Biological Unit (1, 1)
No.NameCountTypeFull Name
1THJ1Ligand/IonTHIOSULFATE

(-) Sites  (1, 1)

Asymmetric Unit (1, 1)
No.NameEvidenceResiduesDescription
1AC1SOFTWAREGLN A:19 , GLY A:23 , SER A:24 , CYS A:25 , GLY A:65 , ASN A:157 , HIS A:158 , HOH A:374 , HOH A:445BINDING SITE FOR RESIDUE THJ A 601

(-) SS Bonds  (3, 3)

Asymmetric/Biological Unit
No.Residues
1A:22 -A:63
2A:56 -A:96
3A:152 -A:203

(-) Cis Peptide Bonds  (1, 1)

Asymmetric/Biological Unit
No.Residues
1Gly A:150 -Pro A:151

 Sequence-Structure Mapping

(-) SAPs(SNPs)/Variants  (0, 0)

(no "SAP(SNP)/Variant" information available for 1IWD)

(-) PROSITE Motifs  (2, 2)

Asymmetric/Biological Unit (2, 2)
 PROSITEUniProtKBPDB
No.IDACDescriptionIDLocationCountLocation
1THIOL_PROTEASE_CYSPS00139 Eukaryotic thiol (cysteine) proteases cysteine active site.ERVB_TABDI19-30  1A:19-30
2THIOL_PROTEASE_ASNPS00640 Eukaryotic thiol (cysteine) proteases asparagine active site.ERVB_TABDI173-192  1A:173-192

(-) Exons   (0, 0)

(no "Exon" information available for 1IWD)

(-) 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    
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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:215
 aligned with ERVB_TABDI | P60994 from UniProtKB/Swiss-Prot  Length:215

    Alignment length:215
                                    10        20        30        40        50        60        70        80        90       100       110       120       130       140       150       160       170       180       190       200       210     
           ERVB_TABDI     1 LPSFVDWRSKGAVNSIKNQKQCGSCWAFSAVAAVESINKIRTGQLISLSEQELVDCDTASHGCNGGWMNNAFQYIITNGGIDTQQNYPYSAVQGSCKPYRLRVVSINGFQRVTRNNESALQSAVASQPVSVTVEAAGAPFQHYSSGIFTGPCGTAQNHGVVIVGYGTQSGKNYWIVRNSWGQNWGNQGYIWMERNVASSAGLCGIAQLPSYPTKA 215
               SCOP domains d1iwda_ A: Ervatamin B                                                                                                                                                                                                  SCOP domains
               CATH domains 1iwdA00 A:1-215 Cysteine proteinases                                                                                                                                                                                    CATH domains
               Pfam domains ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author ....ee.hhhh............hhhhhhhhhhhhhhhhhhhh.....hhhhhhhhh...hhhhh.hhhhhhhhhhhhh............................eeee....hhhhhhhhhhhh.eeeee...hhhhhh....ee.........eeeeeeeeeee..eeeeeee...........eeeee.......hhhhh....eeee.. Sec.struct. author
                 SAPs(SNPs) ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE ------------------THIOL_PROTEA----------------------------------------------------------------------------------------------------------------------------------------------THIOL_PROTEASE_ASN  ----------------------- PROSITE
                 Transcript ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Transcript
                 1iwd A   1 LPSFVDWRSKGAVNSIKNQKQCGSCWAFSAVAAVESINKIRTGQLISLSEQELVDCDTASHGCNGGWMNNAFQYIITNGGIDTQQNYPYSAVQGSCKPYRLRVVSINGFQRVTRNNESALQSAVASQPVSVTVEAAGAPFQHYSSGIFTGPCGTAQNHGVVIVGYGTQSGKNYWIVRNSWGQNWGNQGYIWMERNVASSAGLCGIAQLPSYPTKA 215
                                    10        20        30        40        50        60        70        80        90       100       110       120       130       140       150       160       170       180       190       200       210
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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  (1, 1)

Asymmetric/Biological Unit
(-)
Class: Alpha and beta proteins (a+b) (23004)

(-) CATH Domains  (1, 1)

Asymmetric/Biological Unit
(-)
Class: Alpha Beta (26913)

(-) Pfam Domains  (0, 0)

(no "Pfam Domain" information available for 1IWD)

(-) Gene Ontology  (5, 5)

Asymmetric/Biological Unit(hide GO term definitions)
Chain A   (ERVB_TABDI | P60994)
molecular function
    GO:0008234    cysteine-type peptidase activity    Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile.
    GO:0016787    hydrolase activity    Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. Hydrolase is the systematic name for any enzyme of EC class 3.
    GO:0008233    peptidase activity    Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.
biological process
    GO:0006508    proteolysis    The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
cellular component
    GO:0005576    extracellular region    The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.

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