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1LBU

HYDROLASE METALLO (ZN) DD-PEPTIDASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004180molecular_functioncarboxypeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0009046molecular_functionzinc D-Ala-D-Ala carboxypeptidase activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 214
ChainResidue
AHIS154
AASP161
AHIS197
AHOH234

site_idCAT
Number of Residues4
DetailsTHE ACTIVE SITE.
ChainResidue
AHIS154
AASP161
AHIS197
AZN214

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"6825689","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Blocked amino end (Asp)"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed Charlier2004
ChainResidueDetails
AHIS195
AASP194
AHIS192
ATYR189

site_idMCSA1
Number of Residues7
DetailsM-CSA 585
ChainResidueDetails
AHIS154
AASP161
ATYR189electrostatic stabiliser
AHIS192electrostatic stabiliser
AASP194electrostatic stabiliser, proton shuttle (general acid/base)
AHIS195proton shuttle (general acid/base)
AHIS197

249697

PDB entries from 2026-02-25

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