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2OZ0

Mechanistic and Structural Studies of H373Q Flavocytochrome b2: Effects of Mutating the Active Site Base

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 Residues12
DetailsBINDING SITE FOR RESIDUE HEM A 560
ChainResidue
APHE39
ATYR143
ALEU199
ALEU230
AHIS43
APRO44
AGLY45
AILE50
AHIS66
ATYR74
ATYR97
AGLN139

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE FMN A 569
ChainResidue
ATYR144
ASER195
AALA196
ATHR197
AALA198
ASER228
AGLN252
ATYR254
ATHR280
ALYS349
ASER371
AGLN373
AGLY374
AARG376
AASP409
AGLY410
AGLY411
AARG413
ALEU431
AGLY432
AARG433

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE FMN B 570
ChainResidue
BTYR144
BSER195
BALA196
BTHR197
BALA198
BSER228
BGLN252
BTYR254
BTHR280
BLYS349
BSER371
BGLY374
BARG376
BASP409
BGLY410
BGLY411
BARG413
BLEU431
BGLY432
BARG433
BLEU436
BPYR571

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PYR B 571
ChainResidue
BTYR143
BALA198
BTYR254
BGLN373
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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues77
DetailsDomain: {"description":"Cytochrome b5 heme-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00279","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"17563122","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"11914072","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2329585","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FCB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KBI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues33
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11914072","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2329585","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FCB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KBI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11914072","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KBI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1fcb
ChainResidueDetails
ATYR254
ATYR143
AARG376
AASP282
AGLN373

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1fcb
ChainResidueDetails
BTYR254
BTYR143
BARG376
BASP282
BGLN373

site_idMCSA1
Number of Residues3
DetailsM-CSA 102
ChainResidueDetails
ATYR254electrostatic stabiliser, hydrogen bond donor
AASP282electrostatic stabiliser, hydrogen bond acceptor
AGLN373hydrogen 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
BGLN373hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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PDB entries from 2025-10-08

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