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5WVU

Crystal structure of carboxypeptidase from Thermus thermophilus

Replaces:  1WGZ
Functional Information from GO Data
ChainGOidnamespacecontents
A0004180molecular_functioncarboxypeptidase activity
A0004181molecular_functionmetallocarboxypeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0046872molecular_functionmetal ion binding
B0004180molecular_functioncarboxypeptidase activity
B0004181molecular_functionmetallocarboxypeptidase activity
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0046872molecular_functionmetal ion binding
C0004180molecular_functioncarboxypeptidase activity
C0004181molecular_functionmetallocarboxypeptidase activity
C0006508biological_processproteolysis
C0008237molecular_functionmetallopeptidase activity
C0008270molecular_functionzinc ion binding
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue GOL A 801
ChainResidue
AASP465
AARG468

site_idAC2
Number of Residues5
Detailsbinding site for residue GOL A 802
ChainResidue
AGLN31
AHIS40
AARG43
AALA44
AMET47

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL A 803
ChainResidue
AGLY293
ATHR294
AASP298
AGLN14
ATRP90

site_idAC4
Number of Residues3
Detailsbinding site for residue ZN A 804
ChainResidue
AHIS276
AHIS280
AGLU306

site_idAC5
Number of Residues3
Detailsbinding site for residue ZN B 601
ChainResidue
BHIS276
BHIS280
BGLU306

site_idAC6
Number of Residues6
Detailsbinding site for residue GOL C 601
ChainResidue
CGLN14
CTRP90
CGLY293
CTHR294
CPRO295
CASP298

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN C 602
ChainResidue
CHIS276
CHIS280
CGLU306
CTYR430

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. GTLHEMGHAL
ChainResidueDetails
AGLY273-LEU282

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU01378
ChainResidueDetails
AGLU277
BGLU277
CGLU277

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:15272172
ChainResidueDetails
AHIS276
AHIS280
AGLU306
BHIS276
BHIS280
BGLU306
CHIS276
CHIS280
CGLU306

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PDB entries from 2024-11-06

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