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3RHG

Crystal structure of amidohydrolase pmi1525 (target efi-500319) from proteus mirabilis hi4320

Functional Information from GO Data
ChainGOidnamespacecontents
A0008270molecular_functionzinc ion binding
A0009056biological_processcatabolic process
A0016788molecular_functionhydrolase activity, acting on ester bonds
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 367
ChainResidue
AHIS23
AHIS25
AGLU166
AASP294
ACAC370

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 368
ChainResidue
AGLU166
AHIS199
AHIS229
ACAC370

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BEZ A 369
ChainResidue
AHIS199
AHIS229
APHE261
AASP294
ACAC370
AHOH432
AHOH633
AHOH649
AHOH654

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE CAC A 370
ChainResidue
AHIS23
AHIS25
ATYR126
AGLU166
AHIS199
AHIS229
AASP294
APHE296
AZN367
AZN368
ABEZ369

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 371
ChainResidue
AMET1
ALYS2
AGLY3
ALYS14
AALA344
AGLU345
AHOH388
AHOH406
AHOH588
AHOH719

Functional Information from PROSITE/UniProt
site_idPS01322
Number of Residues9
DetailsPHOSPHOTRIESTERASE_1 Phosphotriesterase family signature 1. GlTLpHEHL
ChainResidueDetails
AGLY18-LEU26

222624

PDB entries from 2024-07-17

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