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2YYL

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

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 Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 700
ChainResidue
ATRP336
AARG338
AHOH1222
AHOH1245

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 701
ChainResidue
AILE73
AARG127
ATYR130
AARG131

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 702
ChainResidue
AGLU260
AARG261
ATYR129

site_idAC4
Number of Residues28
DetailsBINDING SITE FOR RESIDUE FAD A 600
ChainResidue
AHIS142
AALA143
ALEU144
AGLN148
AARG151
ATHR183
ATHR185
AALA312
ATYR315
AHIS317
AGLN378
AILE379
AALA381
ASER382
ALEU436
ATYR437
APHE440
APHE441
AGLY443
AASP444
AARG447
AHOH1084
AHOH1115
AHOH1117
AHOH1150
AHOH1216
AHOH1249
AHOH1512

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

218500

PDB entries from 2024-04-17

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