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4WVZ

Crystal structure of artificial crosslinked thiol dioxygenase G95C variant from Pseudomonas aeruginosa

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0008198molecular_functionferrous iron binding
A0016491molecular_functionoxidoreductase activity
A0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
B0005506molecular_functioniron ion binding
B0008198molecular_functionferrous iron binding
B0016491molecular_functionoxidoreductase activity
B0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
B0046872molecular_functionmetal ion binding
B0051213molecular_functiondioxygenase activity
C0005506molecular_functioniron ion binding
C0008198molecular_functionferrous iron binding
C0016491molecular_functionoxidoreductase activity
C0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
C0046872molecular_functionmetal ion binding
C0051213molecular_functiondioxygenase activity
D0005506molecular_functioniron ion binding
D0008198molecular_functionferrous iron binding
D0016491molecular_functionoxidoreductase activity
D0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
D0046872molecular_functionmetal ion binding
D0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue FE2 A 301
ChainResidue
AHIS89
AHIS91
AHIS142
AHOH402
AHOH536

site_idAC2
Number of Residues5
Detailsbinding site for residue FE2 B 301
ChainResidue
BHOH495
BHIS89
BHIS91
BHIS142
BHOH424

site_idAC3
Number of Residues5
Detailsbinding site for residue FE2 C 301
ChainResidue
CHIS89
CHIS91
CHIS142
CHOH423
CHOH526

site_idAC4
Number of Residues4
Detailsbinding site for residue FE2 D 301
ChainResidue
DHIS89
DHIS91
DHIS142
DHOH455

site_idAC5
Number of Residues14
Detailsbinding site for Di-peptide CYS B 95 and TYR B 159
ChainResidue
BPHE73
BSER74
BHIS91
BVAL93
BTRP94
BLEU96
BALA133
BLEU134
BHIS157
BVAL158
BGLY160
BALA161
BILE163
BHOH424

site_idAC6
Number of Residues15
Detailsbinding site for Di-peptide CYS C 95 and TYR C 159
ChainResidue
CPHE73
CSER74
CPHE78
CHIS91
CVAL93
CTRP94
CLEU96
CALA133
CLEU134
CHIS157
CVAL158
CGLY160
CALA161
CILE163
CHOH423

site_idAC7
Number of Residues15
Detailsbinding site for Di-peptide CYS D 95 and TYR D 159
ChainResidue
DPHE73
DSER74
DPHE78
DHIS91
DVAL93
DTRP94
DLEU96
DALA133
DLEU134
DHIS157
DVAL158
DGLY160
DALA161
DILE163
DHOH455

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26272617","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3USS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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