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1LDC

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 FMN A 570
ChainResidue
ATYR144
ASER371
AHIS373
AGLY374
AARG376
AASP409
AGLY410
AGLY411
AARG413
AGLY432
AARG433
ASER195
APYR580
AHOH608
AHOH612
AALA196
ATHR197
AALA198
ASER228
AGLN252
ATHR280
ALYS349

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEM A 560
ChainResidue
ALEU36
APHE39
AHIS43
APRO44
AVAL49
APHE62
AHIS66
AVAL70
AILE71
AILE75
ATYR97
AGLN139
ALEU199
ALEU230
ALYS296
APYR580

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PYR A 580
ChainResidue
APHE143
ATYR254
AARG289
AHIS373
AARG376
AHEM560
AFMN570

site_idAC4
Number of Residues22
DetailsBINDING SITE FOR RESIDUE FMN B 570
ChainResidue
BPHE143
BTYR144
BSER195
BALA196
BTHR197
BALA198
BSER228
BGLN252
BTYR254
BTHR280
BLYS349
BHIS373
BGLY374
BARG376
BASP409
BGLY410
BGLY411
BARG413
BGLY432
BARG433
BLEU436
BPYR580

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PYR B 580
ChainResidue
BPHE143
BALA198
BTYR254
BARG289
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
BHIS43
BHIS66
AHIS43
AHIS66

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
AGLN252
ATYR254
ATHR280
ALYS349
AHIS373
AARG376
AASP409
AGLY432
BTYR97
BPHE143
BSER195
BSER228
BGLN252
BTYR254
BTHR280
BLYS349
BHIS373
BARG376
BASP409
BGLY432
ATYR97
APHE143
ASER195
ASER228

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

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

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PDB entries from 2024-04-17

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