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1LCO

X-RAY STRUCTURE OF TWO COMPLEXES OF THE Y143F FLAVOCYTOCHROME B2 MUTANT CRYSTALLIZED IN THE PRESENCE OF LACTATE OR PHENYL-LACTATE

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 Residues22
DetailsBINDING SITE FOR RESIDUE HEM A 560
ChainResidue
ALEU36
ALEU65
AHIS66
AALA67
AVAL70
ATYR97
AGLN139
APHE143
ALEU199
ALEU230
AALA231
APHE39
ALYS296
APPY580
AHOH695
AHIS43
APRO44
AVAL49
AILE50
AVAL58
AILE61
APHE62

site_idAC2
Number of Residues26
DetailsBINDING SITE FOR RESIDUE FMN A 570
ChainResidue
ATYR144
ASER195
AALA196
ATHR197
AALA198
ASER228
AGLN252
ATYR254
ATHR280
ALYS349
ASER371
AHIS373
AGLY374
AARG376
AASP409
AGLY410
AGLY411
AARG413
ALEU431
AGLY432
AARG433
ALEU436
APPY580
AHOH610
AHOH618
AHOH636

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PPY A 580
ChainResidue
APHE143
ATYR254
AHIS373
AARG376
AHEM560
AFMN570
AHOH616

site_idAC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE FMN B 570
ChainResidue
BTYR144
BSER195
BALA196
BTHR197
BALA198
BSER228
BGLN252
BTYR254
BTHR280
BLYS349
BHIS373
BGLY374
BARG376
BASP409
BGLY410
BGLY411
BARG413
BGLY432
BARG433
BLEU436
BPPY580

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PPY B 580
ChainResidue
BPHE143
BALA198
BLEU199
BTYR254
BHIS373
BARG376
BFMN570

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
BPHE143
BSER195
BSER228
BGLN252
BTYR254
BTHR280
APHE143
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_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1fcb
ChainResidueDetails
ATYR254
APHE143
AARG376
AASP282
AHIS373

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1fcb
ChainResidueDetails
BTYR254
BPHE143
BARG376
BASP282
BHIS373

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1fcb
ChainResidueDetails
ATYR254
AARG376
AHIS373
AASP282

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1fcb
ChainResidueDetails
BTYR254
BARG376
BHIS373
BASP282

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

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PDB entries from 2024-07-10

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