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1LBU

HYDROLASE METALLO (ZN) DD-PEPTIDASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004180molecular_functioncarboxypeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0009046molecular_functionzinc D-Ala-D-Ala carboxypeptidase 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
DetailsACT_SITE: Proton donor => ECO:0000255
ChainResidueDetails
AHIS192

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AARG138

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:6825689
ChainResidueDetails
AHIS154
AHIS195
AHIS197

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Blocked amino end (Asp)
ChainResidueDetails
AASP1

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

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PDB entries from 2024-07-24

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