1BU7
CRYOGENIC STRUCTURE OF CYTOCHROME P450BM-3 HEME DOMAIN
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0020037 | molecular_function | heme binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0020037 | molecular_function | heme binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM A 999 |
| Chain | Residue |
| A | LYS69 |
| A | PHE393 |
| A | GLY394 |
| A | ARG398 |
| A | ALA399 |
| A | CYS400 |
| A | ILE401 |
| A | GLY402 |
| A | ALA406 |
| A | HOH1020 |
| A | HOH1039 |
| A | LEU86 |
| A | HOH1058 |
| A | HOH1087 |
| A | HOH1093 |
| A | HOH1173 |
| A | HOH1197 |
| A | PHE87 |
| A | TRP96 |
| A | GLY265 |
| A | THR268 |
| A | THR269 |
| A | PHE331 |
| A | PRO392 |
| site_id | AC2 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE HEM B 1000 |
| Chain | Residue |
| B | LYS69 |
| B | LEU86 |
| B | TRP96 |
| B | ALA264 |
| B | GLY265 |
| B | THR268 |
| B | THR269 |
| B | THR327 |
| B | PHE331 |
| B | PRO392 |
| B | PHE393 |
| B | GLY394 |
| B | ARG398 |
| B | ALA399 |
| B | CYS400 |
| B | ILE401 |
| B | GLY402 |
| B | ALA406 |
| B | HOH1023 |
| B | HOH1055 |
| B | HOH1105 |
| B | HOH1144 |
| B | HOH1151 |
| B | HOH1152 |
| B | HOH1380 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 1001 |
| Chain | Residue |
| A | HIS100 |
| A | GLY396 |
| A | GLN397 |
| A | ALA399 |
| A | ILE401 |
| A | HOH1093 |
| A | HOH1399 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 1002 |
| Chain | Residue |
| A | GLU137 |
| A | LYS447 |
| A | ALA448 |
| A | EDO1003 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 1003 |
| Chain | Residue |
| A | TRP130 |
| A | LEU133 |
| A | ALA448 |
| A | EDO1002 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 1004 |
| Chain | Residue |
| B | HIS100 |
| B | GLN397 |
| B | ALA399 |
| B | ILE401 |
| B | HOH1015 |
| B | HOH1151 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 1005 |
| Chain | Residue |
| B | TRP130 |
| B | LEU133 |
| B | ALA448 |
| B | EDO1006 |
| B | HOH1061 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 1006 |
| Chain | Residue |
| B | ASN134 |
| B | GLU137 |
| B | ALA448 |
| B | EDO1005 |
| B | HOH1321 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO B 1007 |
| Chain | Residue |
| B | THR245 |
| B | GLY246 |
| B | GLU247 |
| B | VAL281 |
| B | ASP425 |
| B | ASN428 |
| B | HOH1171 |
| B | HOH1358 |
| B | HOH1392 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 1008 |
| Chain | Residue |
| A | LYS289 |
| A | GLU292 |
| A | GLU293 |
| A | ARG296 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 1009 |
| Chain | Residue |
| B | ARG47 |
| B | SER72 |
| B | GLN73 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 1010 |
| Chain | Residue |
| B | PRO25 |
| B | TYR51 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 1011 |
| Chain | Residue |
| B | LYS31 |
| B | HOH1227 |
| B | GLN27 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 1012 |
| Chain | Residue |
| B | LEU181 |
| B | ILE263 |
| B | ALA264 |
| B | HIS266 |
| B | LEU437 |
| B | HOH1237 |
| B | HOH1429 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 1013 |
| Chain | Residue |
| A | VAL26 |
| A | PRO329 |
| A | GLU435 |
| A | THR436 |
| A | LEU437 |
| A | HOH1262 |
| A | HOH1414 |
| site_id | BC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 1014 |
| Chain | Residue |
| A | TRP90 |
| A | HIS92 |
| A | TYR334 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGnGQRACIG |
| Chain | Residue | Details |
| A | PHE393-GLY402 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15020590, ECO:0007744|PDB:1SMJ |
| Chain | Residue | Details |
| A | LEU52 | |
| B | LEU52 |
| Chain | Residue | Details |
| A | ILE401 | |
| B | ILE401 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | SITE: Important for catalytic activity => ECO:0000305|PubMed:16403573, ECO:0000305|PubMed:7578081 |
| Chain | Residue | Details |
| A | THR269 | |
| B | THR269 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 10051560 |
| Chain | Residue | Details |
| A | THR268 | |
| A | CYS400 | |
| A | PHE393 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 699 |
| Chain | Residue | Details |
| A | THR269 | electrostatic stabiliser, steric role |
| A | GLY394 | electrostatic stabiliser, steric role |
| A | ILE401 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 699 |
| Chain | Residue | Details |
| B | THR269 | electrostatic stabiliser, steric role |
| B | GLY394 | electrostatic stabiliser, steric role |
| B | ILE401 | electrostatic stabiliser |
