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2YYG

Crystal structure of the oxygenase component (HpaB) of 4-hydroxyphenylacetate 3-monooxygenase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0010124biological_processphenylacetate catabolic process
A0016491molecular_functionoxidoreductase activity
A0016627molecular_functionoxidoreductase activity, acting on the CH-CH group of donors
A0016712molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
A0019439biological_processaromatic compound catabolic process
A0050660molecular_functionflavin adenine dinucleotide binding
A0052881molecular_function4-hydroxyphenylacetate 3-monooxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 600
ChainResidue
AGLY231
AASP232
ASER233
AHOH1069
AHOH1182
AHOH1353

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 601
ChainResidue
AHOH1134
ATRP336
ATHR337
AARG338

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 602
ChainResidue
AILE73
AARG127
ATYR130
AARG131
ASO4604

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 603
ChainResidue
ATYR456
ALYS458
AGLU459
ALYS462
AHOH1234

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 604
ChainResidue
AARG131
AARG134
ASO4602

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AARG100
ASER197

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:17804419
ChainResidueDetails
AHIS142
AGLN148
ATHR185
AASP444

217705

PDB entries from 2024-03-27

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