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1P0V

F393A mutant heme domain of flavocytochrome P450 BM3

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0020037molecular_functionheme binding
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0020037molecular_functionheme binding
Functional Information from PDB Data
site_idAC1
Number of Residues27
DetailsBINDING SITE FOR RESIDUE HEM A 460
ChainResidue
ALYS69
ATHR327
APHE331
APRO392
AGLY394
AARG398
AALA399
ACYS400
AILE401
AGLY402
AGLN403
ALEU86
AALA406
AHOH465
AHOH466
AHOH488
AHOH504
AHOH525
AHOH540
AHOH1048
APHE87
ATRP96
AALA264
AGLY265
ATHR268
ATHR269
ALEU272

site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM B 460
ChainResidue
BLYS69
BLEU86
BPHE87
BTRP96
BALA264
BGLY265
BTHR268
BTHR269
BTHR327
BPHE331
BPRO392
BGLY394
BARG398
BALA399
BCYS400
BILE401
BGLY402
BGLN403
BALA406
BHOH464
BHOH466
BHOH474
BHOH484
BHOH531
BHOH560

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15020590, ECO:0007744|PDB:1SMJ
ChainResidueDetails
ALEU52
BLEU52

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:10051560, ECO:0000269|PubMed:11695889, ECO:0000269|PubMed:11695892, ECO:0000269|PubMed:14653735, ECO:0000269|PubMed:15020590, ECO:0000269|PubMed:15299332, ECO:0000269|PubMed:16403573, ECO:0000269|PubMed:17077084, ECO:0000269|PubMed:17429965, ECO:0000269|PubMed:17868686, ECO:0000269|PubMed:18004886, ECO:0000269|PubMed:18298086, ECO:0000269|PubMed:18619466, ECO:0000269|PubMed:18721129, ECO:0000269|PubMed:19492389, ECO:0000269|PubMed:20180779, ECO:0000269|PubMed:20947800, ECO:0000269|PubMed:21110374, ECO:0000269|PubMed:21875028, ECO:0000269|PubMed:7578081, ECO:0000269|PubMed:8342039, ECO:0000269|PubMed:9033595, ECO:0007744|PDB:1BU7, ECO:0007744|PDB:1BVY, ECO:0007744|PDB:1FAG, ECO:0007744|PDB:1FAH, ECO:0007744|PDB:1JME, ECO:0007744|PDB:1JPZ, ECO:0007744|PDB:1P0V, ECO:0007744|PDB:1P0W, ECO:0007744|PDB:1P0X, ECO:0007744|PDB:1SMI, ECO:0007744|PDB:1SMJ, ECO:0007744|PDB:1YQO, ECO:0007744|PDB:1YQP, ECO:0007744|PDB:1ZO4, ECO:0007744|PDB:1ZO9, ECO:0007744|PDB:1ZOA, ECO:0007744|PDB:2BMH, ECO:0007744|PDB:2HPD, ECO:0007744|PDB:2IJ2, ECO:0007744|PDB:2IJ3, ECO:0007744|PDB:2IJ4, ECO:0007744|PDB:2J1M, ECO:0007744|PDB:2J4S, ECO:0007744|PDB:2UWH, ECO:0007744|PDB:3BEN, ECO:0007744|PDB:3CBD, ECO:0007744|PDB:3EKB, ECO:0007744|PDB:3EKD, ECO:0007744|PDB:3EKF, ECO:0007744|PDB:3HF2, ECO:0007744|PDB:3KX3, ECO:0007744|PDB:3KX4, ECO:0007744|PDB:3KX5, ECO:0007744|PDB:3M4V, ECO:0007744|PDB:3NPL
ChainResidueDetails
AILE401
BILE401

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Important for catalytic activity => ECO:0000305|PubMed:16403573, ECO:0000305|PubMed:7578081
ChainResidueDetails
ATHR269
BTHR269

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
ATHR268
AGLU267

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
BTHR268
BGLU267

site_idMCSA1
Number of Residues3
DetailsM-CSA 699
ChainResidueDetails
ATHR269electrostatic stabiliser, steric role
AGLY394electrostatic stabiliser, steric role
AILE401electrostatic stabiliser

site_idMCSA2
Number of Residues3
DetailsM-CSA 699
ChainResidueDetails
BTHR269electrostatic stabiliser, steric role
BGLY394electrostatic stabiliser, steric role
BILE401electrostatic stabiliser

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PDB entries from 2024-07-17

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