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2GV8

Crystal structure of flavin-containing monooxygenase (FMO) from S.pombe and NADPH cofactor complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0004499molecular_functionN,N-dimethylaniline monooxygenase activity
A0005789cellular_componentendoplasmic reticulum membrane
A0050660molecular_functionflavin adenine dinucleotide binding
A0050661molecular_functionNADP binding
A0071949molecular_functionFAD binding
A1990748biological_processcellular detoxification
B0004497molecular_functionmonooxygenase activity
B0004499molecular_functionN,N-dimethylaniline monooxygenase activity
B0005789cellular_componentendoplasmic reticulum membrane
B0050660molecular_functionflavin adenine dinucleotide binding
B0050661molecular_functionNADP binding
B0071949molecular_functionFAD binding
B1990748biological_processcellular detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues37
DetailsBINDING SITE FOR RESIDUE FAD A 500
ChainResidue
AGLY13
ATRP47
APRO83
ALEU84
ALEU88
ATHR90
AASN91
ATHR92
ATHR136
AASP137
AVAL138
AGLY15
ACYS172
AASN173
AGLY174
ATYR176
APHE296
APRO342
APHE343
ANDP501
AHOH503
AHOH508
APRO16
AHOH511
AHOH512
AHOH527
AHOH542
AHOH545
AHOH599
AHOH627
AHOH673
ASER17
AGLU38
AARG39
AARG40
AGLY45
AVAL46

site_idAC2
Number of Residues38
DetailsBINDING SITE FOR RESIDUE FAD B 500
ChainResidue
BGLY13
BGLY15
BPRO16
BSER17
BGLU38
BARG39
BARG40
BGLY45
BVAL46
BTRP47
BPRO83
BLEU84
BLEU88
BTHR90
BASN91
BTHR92
BTHR136
BASP137
BVAL138
BCYS172
BASN173
BGLY174
BTYR176
BPHE296
BPRO342
BPHE343
BNDP501
BHOH503
BHOH508
BHOH511
BHOH529
BHOH531
BHOH532
BHOH539
BHOH562
BHOH570
BHOH622
BHOH626

site_idAC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NDP A 501
ChainResidue
ATYR85
AGLN89
AASN91
ATYR176
AGLY219
AALA221
ASER222
ASER223
AASP226
ASER242
ALEU244
ACYS287
ATHR288
AFAD500
AHOH533
AHOH535
AHOH563
AHOH570
AHOH579
AHOH602
AHOH648
AHOH661
AHOH670
AHOH712

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE NDP B 501
ChainResidue
BTYR85
BGLN89
BASN91
BTYR176
BGLY219
BALA221
BSER222
BSER223
BASP226
BSER242
BLEU244
BCYS287
BTHR288
BGLY289
BFAD500
BHOH573
BHOH576
BHOH594
BHOH648
BHOH672

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 502
ChainResidue
ATYR49
ASER51
AARG86
AGLU206
AHOH509
AHOH653
AHOH654
BASN48
BHOH636
BHOH641

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL B 502
ChainResidue
AASN48
AHOH585
BTYR49
BSER51
BARG86
BGLU206
BHOH505
BHOH631
BHOH632
BHOH702

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:16777962, ECO:0007744|PDB:1VQW, ECO:0007744|PDB:2GV8, ECO:0007744|PDB:2GVC
ChainResidueDetails
BASN91
BASP137
AGLY13
AGLU38
AVAL46
AASN91
AASP137
BGLY13
BGLU38
BVAL46

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:16777962, ECO:0007744|PDB:2GV8
ChainResidueDetails
ATHR90
ASER223
BTHR90
BSER223

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PDB entries from 2024-06-12

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