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2YYK

Crystal structure of the mutant of HpaB (T198I, A276G, and R466H)

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
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 NA A 505
ChainResidue
AGLU226
AHIS237
AHOH1747
AHOH1748
AHOH1749
AHOH1750

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY A 500
ChainResidue
ALEU452
AHOH1784
AARG355
AGLY356
AASP359

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACY A 501
ChainResidue
ALEU144
ATHR145
AASN146
AARG181
APRO196
ASER197
AILE198
AHOH1576

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACY A 502
ChainResidue
AARG82
AHOH1838

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 601
ChainResidue
AARG225
AGLU226
ALEU384
AILE385
ATHR386
ALEU387
AARG420
ATRP423

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17804419","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1u8v
ChainResidueDetails
AMET284

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1u8v
ChainResidueDetails
AASN282

245663

PDB entries from 2025-12-03

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