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1AZW

PROLINE IMINOPEPTIDASE FROM XANTHOMONAS CAMPESTRIS PV. CITRI

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0005737cellular_componentcytoplasm
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
B0004177molecular_functionaminopeptidase activity
B0005737cellular_componentcytoplasm
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
Functional Information from PDB Data
site_idAS
Number of Residues3
DetailsACTIVE-SITE.
ChainResidue
AGLY100
AASP266
AHIS294

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:9427736
ChainResidueDetails
ASER110
BSER110

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:9427736
ChainResidueDetails
AASP266
BASP266

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:9427736
ChainResidueDetails
AHIS294
BHIS294

Catalytic Information from CSA
site_idCSA1
Number of Residues5
Detailsa catalytic site defined by CSA, PubMed 9427736, 11948789, 10467172
ChainResidueDetails
ASER110
AHIS294
AASP266
ATRP111
AGLY43

site_idMCSA1
Number of Residues5
DetailsM-CSA 412
ChainResidueDetails
AGLY43electrostatic stabiliser
ASER110covalent catalysis, proton shuttle (general acid/base)
ATRP111electrostatic stabiliser
AASP266electrostatic stabiliser
AHIS294electrostatic stabiliser, proton shuttle (general acid/base)

site_idMCSA2
Number of Residues5
DetailsM-CSA 412
ChainResidueDetails
BGLY43electrostatic stabiliser
BSER110covalent catalysis, proton shuttle (general acid/base)
BTRP111electrostatic stabiliser
BASP266electrostatic stabiliser
BHIS294electrostatic stabiliser, proton shuttle (general acid/base)

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PDB entries from 2024-08-21

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