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5VRI

Crystal structure of SsoPox AsA6 mutant (F46L-C258A-W263M-I280T) - closed form

Functional Information from GO Data
ChainGOidnamespacecontents
A0004063molecular_functionaryldialkylphosphatase activity
A0008270molecular_functionzinc ion binding
A0009056biological_processcatabolic process
A0016787molecular_functionhydrolase activity
A0016788molecular_functionhydrolase activity, acting on ester bonds
A0046872molecular_functionmetal ion binding
B0004063molecular_functionaryldialkylphosphatase activity
B0008270molecular_functionzinc ion binding
B0009056biological_processcatabolic process
B0016787molecular_functionhydrolase activity
B0016788molecular_functionhydrolase activity, acting on ester bonds
B0046872molecular_functionmetal ion binding
C0004063molecular_functionaryldialkylphosphatase activity
C0008270molecular_functionzinc ion binding
C0009056biological_processcatabolic process
C0016787molecular_functionhydrolase activity
C0016788molecular_functionhydrolase activity, acting on ester bonds
C0046872molecular_functionmetal ion binding
D0004063molecular_functionaryldialkylphosphatase activity
D0008270molecular_functionzinc ion binding
D0009056biological_processcatabolic process
D0016787molecular_functionhydrolase activity
D0016788molecular_functionhydrolase activity, acting on ester bonds
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue CO A 401
ChainResidue
AKCX137
AHIS170
AHIS199
AFE2402
AHOH530

site_idAC2
Number of Residues6
Detailsbinding site for residue FE2 A 402
ChainResidue
ACO401
AHOH530
AHIS22
AHIS24
AKCX137
AASP256

site_idAC3
Number of Residues1
Detailsbinding site for residue EDO A 403
ChainResidue
AASP256

site_idAC4
Number of Residues6
Detailsbinding site for residue GOL A 404
ChainResidue
AASN160
ALYS164
AGLY189
AVAL190
AASP191
AHOH558

site_idAC5
Number of Residues5
Detailsbinding site for residue CO B 401
ChainResidue
BKCX137
BHIS170
BHIS199
BFE2402
BHOH523

site_idAC6
Number of Residues6
Detailsbinding site for residue FE2 B 402
ChainResidue
BHIS22
BHIS24
BKCX137
BASP256
BCO401
BHOH523

site_idAC7
Number of Residues7
Detailsbinding site for residue GOL B 403
ChainResidue
BALA213
BASP214
BGLY246
BTYR247
BASP249
BLYS250
BHOH528

site_idAC8
Number of Residues2
Detailsbinding site for residue EDO B 404
ChainResidue
BASP256
BHOH518

site_idAC9
Number of Residues5
Detailsbinding site for residue GOL B 405
ChainResidue
BASN160
BLYS164
BGLY189
BASP191
BHOH536

site_idAD1
Number of Residues5
Detailsbinding site for residue CO C 401
ChainResidue
CKCX137
CHIS170
CHIS199
CFE2402
CHOH506

site_idAD2
Number of Residues6
Detailsbinding site for residue FE2 C 402
ChainResidue
CHIS22
CHIS24
CKCX137
CASP256
CCO401
CHOH506

site_idAD3
Number of Residues2
Detailsbinding site for residue EDO C 403
ChainResidue
CASP256
CHOH599

site_idAD4
Number of Residues5
Detailsbinding site for residue GOL C 404
ChainResidue
CASN160
CLYS164
CGLY189
CASP191
CLYS194

site_idAD5
Number of Residues5
Detailsbinding site for residue CO D 401
ChainResidue
DKCX137
DHIS170
DHIS199
DFE2402
DHOH506

site_idAD6
Number of Residues6
Detailsbinding site for residue FE2 D 402
ChainResidue
DHIS22
DHIS24
DKCX137
DASP256
DCO401
DHOH506

site_idAD7
Number of Residues4
Detailsbinding site for residue GOL D 403
ChainResidue
DASN160
DGLY189
DVAL190
DASP191

site_idAD8
Number of Residues3
Detailsbinding site for residue EDO D 404
ChainResidue
DASP256
DTRP278
DHOH610

Functional Information from PROSITE/UniProt
site_idPS01322
Number of Residues9
DetailsPHOSPHOTRIESTERASE_1 Phosphotriesterase family signature 1. GfTLiHEHL
ChainResidueDetails
AGLY17-LEU25

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18486146","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2VC5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2VC7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UF9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KER","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KES","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KET","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KEU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KEV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KEZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KF1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"description":"via carbamate group","evidences":[{"source":"PubMed","id":"18486146","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2VC5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2VC7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UF9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KER","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KES","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KET","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KEU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KEV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KEZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KF1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00679","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18486146","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2VC5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2VC7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UF9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KER","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KES","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KET","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KEU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KEV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KEZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KF1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

249697

PDB entries from 2026-02-25

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