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1GQW

Taurine/alpha-ketoglutarate Dioxygenase from Escherichia coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0000908molecular_functiontaurine dioxygenase activity
A0005737cellular_componentcytoplasm
A0006790biological_processsulfur compound metabolic process
A0008198molecular_functionferrous iron binding
A0016491molecular_functionoxidoreductase activity
A0016706molecular_function2-oxoglutarate-dependent dioxygenase activity
A0019529biological_processtaurine catabolic process
A0031418molecular_functionL-ascorbic acid binding
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
A0051289biological_processprotein homotetramerization
A1990205cellular_componenttaurine dioxygenase complex
B0000908molecular_functiontaurine dioxygenase activity
B0005737cellular_componentcytoplasm
B0006790biological_processsulfur compound metabolic process
B0008198molecular_functionferrous iron binding
B0016491molecular_functionoxidoreductase activity
B0016706molecular_function2-oxoglutarate-dependent dioxygenase activity
B0019529biological_processtaurine catabolic process
B0031418molecular_functionL-ascorbic acid binding
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0051213molecular_functiondioxygenase activity
B0051289biological_processprotein homotetramerization
B1990205cellular_componenttaurine dioxygenase complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE2 A 301
ChainResidue
AHIS99
AASP101
AHIS255
AAKG352

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE2 B 301
ChainResidue
BHIS99
BASP101
BHIS255
BAKG352

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE TAU A 351
ChainResidue
ATYR73
AASN95
AHIS99
AASP101
AVAL102
ASER158
APHE159
APHE206
AARG270
AHIS70

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE AKG A 352
ChainResidue
ALEU85
AASN95
AHIS99
AASP101
ALEU114
ATHR126
ATRP240
AHIS255
AARG266
AMET268
AARG270
AFE2301

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE TAU B 351
ChainResidue
BHIS70
BTYR73
BASN95
BASP101
BVAL102
BPHE104
BSER158
BPHE159
BPHE206
BARG270

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE AKG B 352
ChainResidue
BLEU85
BASN95
BHIS99
BASP101
BLEU114
BTHR126
BTRP240
BHIS255
BARG266
BMET268
BARG270
BFE2301

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBINDING: BINDING => ECO:0000269|PubMed:11955067, ECO:0000269|PubMed:12741810
ChainResidueDetails
AHIS70
AARG270
BHIS70
BTYR73
BASN95
BHIS99
BASP101
BVAL102
BTHR126
BHIS255
BARG266
ATYR73
BARG270
AASN95
AHIS99
AASP101
AVAL102
ATHR126
AHIS255
AARG266

site_idSWS_FT_FI2
Number of Residues6
DetailsMOD_RES: 3-hydroxytryptophan; by autocatalysis => ECO:0000269|PubMed:11955067
ChainResidueDetails
ATRP128
ATRP240
ATRP248
BTRP128
BTRP240
BTRP248

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 129
ChainResidueDetails
AHIS99metal ligand
AASP101metal ligand
AHIS255metal ligand
AARG270electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues4
DetailsM-CSA 129
ChainResidueDetails
BHIS99metal ligand
BASP101metal ligand
BHIS255metal ligand
BARG270electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2025-06-11

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