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3SZY

Crystal Structure of Phosphonoacetate hydrolase from Sinorhizobium meliloti 1021 in APO form

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0047400molecular_functionphosphonoacetate hydrolase activity
A0047429molecular_functionnucleoside triphosphate diphosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
AASP29
ATHR68
AASP211
AASP250
AHIS251

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 502
ChainResidue
AASP211
AHIS215
AHIS377

Functional Information from PROSITE/UniProt
site_idPS00133
Number of Residues11
DetailsCARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HGGLTEQeVPF
ChainResidueDetails
AHIS377-PHE387

247536

PDB entries from 2026-01-14

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