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3PSX

Crystal structure of the KT2 mutant of cytochrome 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 Residues28
DetailsBINDING SITE FOR RESIDUE HEM A 482
ChainResidue
ALYS69
ATHR327
APHE331
APRO392
APHE393
AGLY394
AARG398
AALA399
ACYS400
AILE401
AGLY402
ALEU86
APHE405
AALA406
AHOH499
AHOH504
AHOH563
AHOH585
AHOH640
AHOH741
AHOH868
APHE87
ATRP96
AALA264
AGLY265
ATHR268
ATHR269
ALEU322

site_idAC2
Number of Residues28
DetailsBINDING SITE FOR RESIDUE HEM B 482
ChainResidue
BLYS69
BLEU86
BPHE87
BTRP96
BPHE107
BPHE261
BALA264
BGLY265
BTHR268
BTHR269
BLEU272
BTHR327
BPHE331
BPRO392
BPHE393
BGLY394
BARG398
BALA399
BCYS400
BILE401
BGLY402
BHOH508
BHOH538
BHOH601
BHOH624
BHOH705
BHOH870
BHOH914

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGnGQRACIG
ChainResidueDetails
APHE393-GLY402

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15020590, ECO:0007744|PDB:1SMJ
ChainResidueDetails
ATYR51
BTYR51

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
ACYS400
BCYS400

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Important for catalytic activity => ECO:0000305|PubMed:16403573, ECO:0000305|PubMed:7578081
ChainResidueDetails
ATHR268
BTHR268

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 699
ChainResidueDetails
ATHR268electrostatic stabiliser, steric role
APHE393electrostatic stabiliser, steric role
ACYS400electrostatic stabiliser

site_idMCSA2
Number of Residues3
DetailsM-CSA 699
ChainResidueDetails
BTHR268electrostatic stabiliser, steric role
BPHE393electrostatic stabiliser, steric role
BCYS400electrostatic stabiliser

217705

数据于2024-03-27公开中

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