Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0020037 | molecular_function | heme binding |
B | 0020037 | molecular_function | heme binding |
C | 0020037 | molecular_function | heme binding |
D | 0020037 | molecular_function | heme binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE HEM A 200 |
Chain | Residue |
A | MET1 |
A | SER133 |
A | ARG135 |
A | MET137 |
A | LEU144 |
A | OXY493 |
A | HOH508 |
A | HOH509 |
A | HOH548 |
A | HOH555 |
A | LYS2 |
A | PHE94 |
A | MET98 |
A | HIS102 |
A | LEU105 |
A | ALA115 |
A | LEU117 |
A | TYR131 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE OXY A 493 |
Chain | Residue |
A | ILE5 |
A | TYR140 |
A | LEU144 |
A | HEM200 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 494 |
Chain | Residue |
A | ASP45 |
A | VAL48 |
A | TRP67 |
site_id | AC4 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE HEM B 200 |
Chain | Residue |
B | MET1 |
B | LYS2 |
B | PHE78 |
B | PHE86 |
B | PHE94 |
B | MET98 |
B | HIS102 |
B | LEU105 |
B | THR106 |
B | ALA115 |
B | LEU117 |
B | TYR131 |
B | SER133 |
B | ARG135 |
B | LEU144 |
B | ILE145 |
B | OXY494 |
B | HOH510 |
B | HOH518 |
B | HOH547 |
B | HOH549 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE OXY B 494 |
Chain | Residue |
B | TYR140 |
B | HEM200 |
site_id | AC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL B 495 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 496 |
Chain | Residue |
B | MET1 |
B | ASP45 |
B | VAL48 |
B | TRP67 |
B | MET137 |
B | HOH538 |
site_id | AC8 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE HEM C 200 |
Chain | Residue |
C | LYS2 |
C | TYR85 |
C | PHE94 |
C | MET98 |
C | HIS102 |
C | LEU105 |
C | THR106 |
C | ALA115 |
C | TYR131 |
C | SER133 |
C | ARG135 |
C | LEU144 |
C | ILE145 |
C | OXY495 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE OXY C 495 |
Chain | Residue |
C | ILE5 |
C | PHE78 |
C | TYR140 |
C | HEM200 |
site_id | BC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL C 496 |
site_id | BC2 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE HEM D 200 |
Chain | Residue |
D | MET1 |
D | LYS2 |
D | PHE78 |
D | PHE82 |
D | TYR85 |
D | PHE94 |
D | MET98 |
D | HIS102 |
D | LEU105 |
D | ALA115 |
D | LEU117 |
D | MET129 |
D | TYR131 |
D | SER133 |
D | ARG135 |
D | MET137 |
D | LEU144 |
D | OXY496 |
D | HOH508 |
D | HOH511 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE OXY D 496 |
Chain | Residue |
D | PHE78 |
D | TYR140 |
D | LEU144 |
D | HEM200 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 D 497 |
Chain | Residue |
D | ASP45 |
D | ARG49 |
D | HOH514 |
D | MET1 |
Functional Information from PROSITE/UniProt
site_id | PS00217 |
Number of Residues | 26 |
Details | SUGAR_TRANSPORT_2 Sugar transport proteins signature 2. FlGLIeGSskffkeeIsvEevergeK |
Chain | Residue | Details |
A | PHE141-LYS166 | |