Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1KBI

Crystallographic Study of the Recombinant Flavin-binding Domain of Baker's Yeast Flavocytochrome b2: Comparison with the Intact Wild-type Enzyme

Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
A0020037molecular_functionheme binding
B0016491molecular_functionoxidoreductase activity
B0020037molecular_functionheme binding
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM A 760
ChainResidue
ALEU36
AHIS66
AVAL70
AILE71
ATYR97
AGLN139
ATYR143
AALA198
ALEU199
ALEU230
ALYS296
APHE39
AHOH797
AHOH807
AHOH858
AHOH871
AHIS43
APRO44
AGLY45
AVAL49
AVAL58
AILE61
APHE62

site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE FMN A 770
ChainResidue
ATYR143
ATYR144
ASER195
AALA196
ATHR197
AALA198
ASER228
AGLN252
ATYR254
ATHR280
ALYS349
ASER371
AHIS373
AGLY374
AARG376
AASP409
AGLY410
AGLY411
AARG413
AGLY432
AARG433
ALEU436
AHOH771
AHOH797
AHOH814

site_idAC3
Number of Residues26
DetailsBINDING SITE FOR RESIDUE FMN B 870
ChainResidue
BTYR143
BTYR144
BSER195
BALA196
BTHR197
BALA198
BSER228
BGLN252
BTYR254
BTHR280
BLYS349
BSER371
BHIS373
BGLY374
BARG376
BASP409
BGLY410
BGLY411
BARG413
BLEU431
BGLY432
BARG433
BLEU436
BPYR800
BHOH901
BHOH908

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PYR B 800
ChainResidue
BTYR143
BTYR254
BHIS373
BARG376
BFMN870
BHOH1020

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD A 701
ChainResidue
AARG259
AASP263
AASP334
AGLU337
ALYS341
AHOH937

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD A 702
ChainResidue
AARG353
AGLU355
ALYS359
AHOH948
BLYS169
BASP476

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MPD A 703
ChainResidue
AGLY185

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD A 704
ChainResidue
AGLU355
AGLU390
AILE394
AARG398

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD B 801
ChainResidue
BASP263
BASP334
BLEU338
BARG259
BTHR262

Functional Information from PROSITE/UniProt
site_idPS00191
Number of Residues8
DetailsCYTOCHROME_B5_1 Cytochrome b5 family, heme-binding domain signature. FLPNHPGG
ChainResidueDetails
APHE39-GLY46

site_idPS00557
Number of Residues7
DetailsFMN_HYDROXY_ACID_DH_1 FMN-dependent alpha-hydroxy acid dehydrogenases active site. SNHGGRQ
ChainResidueDetails
ASER371-GLN377

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:17563122
ChainResidueDetails
AHIS373
BHIS373

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:11914072, ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, ECO:0007744|PDB:1KBI
ChainResidueDetails
AHIS43
AHIS66
BHIS43
BHIS66

site_idSWS_FT_FI3
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:11914072, ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, ECO:0007744|PDB:1KBI
ChainResidueDetails
ATYR97
AARG376
AASP409
AGLY432
BTYR97
BTYR143
BSER195
BSER228
BGLN252
BTYR254
BTHR280
ATYR143
BLYS349
BHIS373
BARG376
BASP409
BGLY432
ASER195
ASER228
AGLN252
ATYR254
ATHR280
ALYS349
AHIS373

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:11914072, ECO:0007744|PDB:1KBI
ChainResidueDetails
AGLN139
ALYS296
BGLN139
BLYS296

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 102
ChainResidueDetails
ATYR254electrostatic stabiliser, hydrogen bond donor
AASP282electrostatic stabiliser, hydrogen bond acceptor
AHIS373hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_idMCSA2
Number of Residues3
DetailsM-CSA 102
ChainResidueDetails
BTYR254electrostatic stabiliser, hydrogen bond donor
BASP282electrostatic stabiliser, hydrogen bond acceptor
BHIS373hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon