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4UDR

Crystal structure of the H467A mutant of 5-hydroxymethylfurfural oxidase (HMFO)

Functional Information from GO Data
ChainGOidnamespacecontents
A0008812molecular_functioncholine dehydrogenase activity
A0016491molecular_functionoxidoreductase activity
A0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
A0016670molecular_functionoxidoreductase activity, acting on a sulfur group of donors, oxygen as acceptor
A0016899molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor
A0019285biological_processglycine betaine biosynthetic process from choline
A0050660molecular_functionflavin adenine dinucleotide binding
A0055114biological_processobsolete oxidation-reduction process
A0071949molecular_functionFAD binding
B0008812molecular_functioncholine dehydrogenase activity
B0016491molecular_functionoxidoreductase activity
B0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
B0016670molecular_functionoxidoreductase activity, acting on a sulfur group of donors, oxygen as acceptor
B0016899molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor
B0019285biological_processglycine betaine biosynthetic process from choline
B0050660molecular_functionflavin adenine dinucleotide binding
B0055114biological_processobsolete oxidation-reduction process
B0071949molecular_functionFAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues39
DetailsBINDING SITE FOR RESIDUE FAD A 700
ChainResidue
AGLY12
AARG93
ALEU94
AGLY97
AGLY98
AVAL101
AASN102
AMET103
AVAL104
AVAL105
ASER231
AGLY14
AVAL233
ATHR265
AALA266
AGLY267
ATRP466
AASP500
AALA501
AASN511
ATHR512
AASN513
ATHR15
ATHR516
AHOH2007
AHOH2123
AHOH2125
AHOH2126
AHOH2131
AHOH2294
AHOH2297
AHOH2433
AHOH2435
AALA16
AGLU36
AALA37
ATRP68
AGLU90
AGLY92

site_idAC2
Number of Residues41
DetailsBINDING SITE FOR RESIDUE FAD B 700
ChainResidue
BGLY12
BGLY14
BTHR15
BALA16
BILE35
BGLU36
BALA37
BTRP68
BGLU90
BGLY92
BARG93
BLEU94
BGLY97
BGLY98
BVAL101
BASN102
BMET103
BVAL104
BVAL105
BSER231
BARG232
BVAL233
BTHR265
BALA266
BGLY267
BTRP466
BASP500
BALA501
BASN511
BTHR512
BASN513
BTHR516
BHOH2005
BHOH2077
BHOH2078
BHOH2079
BHOH2086
BHOH2228
BHOH2231
BHOH2350
BHOH2351

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT B 1530
ChainResidue
BTHR72
BILE73
BASP391
BVAL392

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FMT A 1530
ChainResidue
AARG297
AALA477
AASP479
ASER480

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:24271187, ECO:0000305|DOI:10.1021/ACSCATAL.5B00031
ChainResidueDetails
AALA467
BALA467

site_idSWS_FT_FI2
Number of Residues18
DetailsBINDING: BINDING => ECO:0000305|DOI:10.1021/ACSCATAL.5B00031, ECO:0007744|PDB:4UDP, ECO:0007744|PDB:4UDQ, ECO:0007744|PDB:4UDR
ChainResidueDetails
ATHR15
BTHR15
BGLU36
BTRP68
BLEU94
BGLY98
BASN102
BVAL233
BALA501
BTHR512
AGLU36
ATRP68
ALEU94
AGLY98
AASN102
AVAL233
AALA501
ATHR512

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:4UDR
ChainResidueDetails
ATRP466
BTRP466

222036

PDB entries from 2024-07-03

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