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4ZWU

Crystal structure of organophosphate anhydrolase/prolidase mutant Y212F, V342L, I215Y

Functional Information from GO Data
ChainGOidnamespacecontents
A0016795molecular_functionphosphoric triester hydrolase activity
B0016795molecular_functionphosphoric triester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue MN A 501
ChainResidue
AASP255
AHIS336
AGLU381
AGLU420
AMN502
AHOH638
AHOH774

site_idAC2
Number of Residues6
Detailsbinding site for residue MN A 502
ChainResidue
ATHR257
AGLU420
AMN501
AHOH638
AASP244
AASP255

site_idAC3
Number of Residues2
Detailsbinding site for residue BA A 503
ChainResidue
AASP29
AHOH772

site_idAC4
Number of Residues1
Detailsbinding site for residue MN A 504
ChainResidue
AASP29

site_idAC5
Number of Residues9
Detailsbinding site for residue GOA B 501
ChainResidue
BPHE212
BASP244
BASP255
BHIS336
BHIS343
BGLU381
BMN503
BMN504
BHOH607

site_idAC6
Number of Residues2
Detailsbinding site for residue GOL B 502
ChainResidue
AASP309
AASN311

site_idAC7
Number of Residues7
Detailsbinding site for residue MN B 503
ChainResidue
BASP244
BASP255
BTHR257
BGLU420
BGOA501
BMN504
BHOH607

site_idAC8
Number of Residues7
Detailsbinding site for residue MN B 504
ChainResidue
BASP255
BHIS336
BGLU381
BGLU420
BGOA501
BMN503
BHOH607

site_idAC9
Number of Residues2
Detailsbinding site for residue MN B 505
ChainResidue
BGLU10
BASP398

site_idAD1
Number of Residues3
Detailsbinding site for residue BA B 506
ChainResidue
AHOH803
BASN27
BHOH612

Functional Information from PROSITE/UniProt
site_idPS00491
Number of Residues13
DetailsPROLINE_PEPTIDASE Aminopeptidase P and proline dipeptidase signature. HGLGHhIGLqLHD
ChainResidueDetails
AHIS332-ASP344

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASP244
BGLU420
AASP255
AHIS336
AGLU381
AGLU420
BASP244
BASP255
BHIS336
BGLU381

224004

PDB entries from 2024-08-21

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