3KP0
Crystal Structure of ORNITHINE 4,5 AMINOMUTASE in complex with 2,4-diaminobutyrate (DAB) (Aerobic)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0031419 | molecular_function | cobalamin binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0046983 | molecular_function | protein dimerization activity |
| A | 0047831 | molecular_function | D-ornithine 4,5-aminomutase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0031419 | molecular_function | cobalamin binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0046983 | molecular_function | protein dimerization activity |
| B | 0047831 | molecular_function | D-ornithine 4,5-aminomutase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0031419 | molecular_function | cobalamin binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0046983 | molecular_function | protein dimerization activity |
| C | 0047831 | molecular_function | D-ornithine 4,5-aminomutase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0031419 | molecular_function | cobalamin binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0046983 | molecular_function | protein dimerization activity |
| D | 0047831 | molecular_function | D-ornithine 4,5-aminomutase activity |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0016853 | molecular_function | isomerase activity |
| E | 0031419 | molecular_function | cobalamin binding |
| E | 0047831 | molecular_function | D-ornithine 4,5-aminomutase activity |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0016853 | molecular_function | isomerase activity |
| F | 0031419 | molecular_function | cobalamin binding |
| F | 0047831 | molecular_function | D-ornithine 4,5-aminomutase activity |
| G | 0003824 | molecular_function | catalytic activity |
| G | 0016853 | molecular_function | isomerase activity |
| G | 0031419 | molecular_function | cobalamin binding |
| G | 0047831 | molecular_function | D-ornithine 4,5-aminomutase activity |
| H | 0003824 | molecular_function | catalytic activity |
| H | 0016853 | molecular_function | isomerase activity |
| H | 0031419 | molecular_function | cobalamin binding |
| H | 0047831 | molecular_function | D-ornithine 4,5-aminomutase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE B12 C 1801 |
| Chain | Residue |
| A | TYR116 |
| C | ALA666 |
| C | SER667 |
| C | ILE669 |
| C | ILE670 |
| C | SER671 |
| C | HIS672 |
| C | GLY701 |
| C | GLY702 |
| C | THR703 |
| C | PHE719 |
| A | 5AD1500 |
| C | GLY720 |
| C | SER723 |
| C | VAL728 |
| C | GLU615 |
| C | GLU617 |
| C | HIS618 |
| C | SER619 |
| C | VAL620 |
| C | GLY621 |
| C | LEU622 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE 5AD A 1500 |
| Chain | Residue |
| A | LEU489 |
| A | ASP490 |
| C | B121801 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE B12 B 1801 |
| Chain | Residue |
| B | GLU615 |
| B | GLU617 |
| B | HIS618 |
| B | SER619 |
| B | VAL620 |
| B | GLY621 |
| B | VAL625 |
| B | LEU665 |
| B | ALA666 |
| B | SER667 |
| B | ILE669 |
| B | ILE670 |
| B | SER671 |
| B | HIS672 |
| B | GLY701 |
| B | GLY702 |
| B | THR703 |
| B | PHE719 |
| B | GLY720 |
| B | SER723 |
| B | VAL728 |
| D | TYR116 |
| D | ASP490 |
| D | 5AD1500 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE 5AD D 1500 |
| Chain | Residue |
| B | B121801 |
| D | LEU489 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE Z98 B 767 |
| Chain | Residue |
| B | GLU81 |
| B | ARG109 |
| B | SER114 |
| B | TYR160 |
| B | SER162 |
| B | HIS182 |
| B | TYR187 |
| B | ARG192 |
| B | HIS225 |
| B | ASN226 |
| B | ARG297 |
| B | GLN299 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE Z98 D 767 |
| Chain | Residue |
| B | LYS629 |
| D | GLU81 |
| D | ARG109 |
| D | SER114 |
| D | SER162 |
| D | HIS182 |
| D | TYR187 |
| D | GLY223 |
| D | HIS225 |
| D | ASN226 |
| D | ARG297 |
| D | GLN299 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE Z98 A 767 |
| Chain | Residue |
| A | GLU81 |
| A | ARG109 |
| A | SER114 |
| A | TYR160 |
| A | SER162 |
| A | HIS182 |
| A | TYR187 |
| A | GLY223 |
| A | HIS225 |
| A | ASN226 |
| A | ARG297 |
| A | GLN299 |
| C | LYS629 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE Z98 C 767 |
| Chain | Residue |
| C | HIS225 |
| C | ASN226 |
| C | ARG297 |
| C | GLN299 |
| C | GLU81 |
| C | MET106 |
| C | ARG109 |
| C | SER114 |
| C | TYR160 |
| C | SER162 |
| C | HIS182 |
| C | TYR187 |
| C | ARG192 |
| C | ASP219 |
| C | GLY223 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20106986","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"20106986","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"20106986","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
