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6D61

Crystal structure of 3-hydroxyanthranilate-3,4-dioxygenase I142P from Cupriavidus metallidurans in complex with 4-Cl-3-HAA

Functional Information from GO Data
ChainGOidnamespacecontents
A0000334molecular_function3-hydroxyanthranilate 3,4-dioxygenase activity
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0006569biological_processtryptophan catabolic process
A0008198molecular_functionferrous iron binding
A0009435biological_processNAD biosynthetic process
A0019363biological_processpyridine nucleotide biosynthetic process
A0019805biological_processquinolinate biosynthetic process
A0034354biological_process'de novo' NAD biosynthetic process from tryptophan
A0043420biological_processanthranilate metabolic process
A0046872molecular_functionmetal ion binding
A0046874biological_processquinolinate metabolic process
A0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue FE2 A 201
ChainResidue
AHIS51
AGLU57
AHIS95
AHOH336
AHOH345

site_idAC2
Number of Residues4
Detailsbinding site for residue FE2 A 202
ChainResidue
ACYS125
ACYS128
ACYS162
ACYS165

site_idAC3
Number of Residues11
Detailsbinding site for residue 4AA A 203
ChainResidue
AVAL41
APHE59
APRO97
AARG99
AVAL108
AGLU110
AHOH302
AHOH336
AHOH345
AHOH379
AHOH543

site_idAC4
Number of Residues8
Detailsbinding site for residue TRS A 204
ChainResidue
AVAL132
AHIS133
AASP158
ALYS159
AARG161
APRO163
AHOH349
AHOH356

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING:
ChainResidueDetails
AHIS95
AARG99
AGLU110
ACYS125
ACYS128
ACYS162
ACYS165
AARG47
AHIS51
AGLU57

221051

PDB entries from 2024-06-12

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