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1YFW

Crystal structure of 3-hydroxyanthranilate-3,4-dioxygenase from Ralstonia metallidurans complexed with 4-chloro-3-hydroxyanthranilic acid and O2

Functional Information from GO Data
ChainGOidnamespacecontents
A0000334molecular_function3-hydroxyanthranilate 3,4-dioxygenase activity
A0005506molecular_functioniron ion binding
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
A0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 300
ChainResidue
AHIS51
AGLU57
AHIS95
AOXY310
A4AA401

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE A 301
ChainResidue
ACYS125
ACYS128
ACYS162
ACYS165

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE OXY A 310
ChainResidue
AARG47
AHIS51
AHIS95
APRO97
AFE300
A4AA401

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE TRS A 400
ChainResidue
AVAL132
AHIS133
AASP158
ALYS159
AARG161
APRO163
AHOH430

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 4AA A 401
ChainResidue
AVAL25
AVAL41
AARG47
AHIS51
AGLU57
APHE59
APRO97
AARG99
AGLU110
AILE142
AFE300
AOXY310
AHOH485

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

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PDB entries from 2024-07-17

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