3KOY
Crystal Structure of ornithine 4,5 aminomutase in complex with ornithine (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 A 1801 |
| Chain | Residue |
| A | GLU615 |
| A | ILE670 |
| A | SER671 |
| A | HIS672 |
| A | GLY701 |
| A | GLY702 |
| A | THR703 |
| A | PHE719 |
| A | GLY722 |
| A | SER723 |
| A | VAL728 |
| A | GLU617 |
| C | TYR116 |
| C | ASP490 |
| C | 5AD1500 |
| A | HIS618 |
| A | SER619 |
| A | VAL620 |
| A | GLY621 |
| A | VAL625 |
| A | SER667 |
| A | ILE669 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE 5AD C 1500 |
| Chain | Residue |
| A | B121801 |
| C | LEU489 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE Z97 C 767 |
| Chain | Residue |
| A | LYS629 |
| C | GLU81 |
| C | ARG109 |
| C | GLN113 |
| C | SER114 |
| C | TYR160 |
| C | SER162 |
| C | HIS182 |
| C | TYR187 |
| C | ARG192 |
| C | HIS225 |
| C | ASN226 |
| C | ARG297 |
| C | GLN299 |
| site_id | AC4 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE B12 D 1801 |
| Chain | Residue |
| B | TYR116 |
| B | 5AD1500 |
| D | GLU617 |
| D | HIS618 |
| D | SER619 |
| D | VAL620 |
| D | GLY621 |
| D | LEU622 |
| D | GLU624 |
| D | VAL625 |
| D | ALA666 |
| D | SER667 |
| D | ILE669 |
| D | ILE670 |
| D | SER671 |
| D | HIS672 |
| D | GLY701 |
| D | GLY702 |
| D | THR703 |
| D | PHE719 |
| D | GLY720 |
| D | GLY722 |
| D | SER723 |
| D | VAL728 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE 5AD B 1500 |
| Chain | Residue |
| B | LEU489 |
| B | ASP490 |
| D | B121801 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE Z97 A 767 |
| Chain | Residue |
| A | GLU81 |
| A | ARG109 |
| A | GLY112 |
| A | GLN113 |
| A | SER114 |
| A | TYR160 |
| A | SER162 |
| A | HIS182 |
| A | TYR187 |
| A | ARG192 |
| A | HIS225 |
| A | ASN226 |
| A | ARG297 |
| A | GLN299 |
| C | LYS629 |
| site_id | AC7 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE B12 C 1801 |
| Chain | Residue |
| C | GLY720 |
| C | GLY722 |
| C | SER723 |
| C | VAL728 |
| A | TYR116 |
| A | ASP490 |
| A | 5AD1500 |
| C | GLU615 |
| C | GLU617 |
| C | HIS618 |
| C | SER619 |
| C | VAL620 |
| C | GLY621 |
| C | LEU622 |
| C | SER667 |
| C | ILE669 |
| C | ILE670 |
| C | SER671 |
| C | HIS672 |
| C | GLY701 |
| C | GLY702 |
| C | THR703 |
| C | PHE719 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE 5AD A 1500 |
| Chain | Residue |
| A | LEU489 |
| A | ASP490 |
| C | B121801 |
| site_id | AC9 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE Z97 B 767 |
| Chain | Residue |
| B | GLU81 |
| B | ILE108 |
| B | ARG109 |
| B | GLN113 |
| B | SER114 |
| B | TYR160 |
| B | SER162 |
| B | HIS182 |
| B | TYR187 |
| B | ARG192 |
| B | GLY223 |
| B | HIS225 |
| B | ASN226 |
| B | ARG297 |
| B | GLN299 |
| D | LYS629 |
| site_id | BC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE B12 B 1801 |
| Chain | Residue |
| B | GLU615 |
| B | ASP616 |
| B | GLU617 |
| B | HIS618 |
| B | SER619 |
| B | VAL620 |
| B | GLY621 |
| 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 |
| D | TYR116 |
| D | ASP490 |
| D | 5AD1500 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE 5AD D 1500 |
| Chain | Residue |
| B | B121801 |
| D | LEU489 |
| site_id | BC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE Z97 D 767 |
| Chain | Residue |
| B | LYS629 |
| D | GLU81 |
| D | ARG109 |
| D | GLY112 |
| D | GLN113 |
| D | SER114 |
| D | TYR160 |
| D | SER162 |
| D | HIS182 |
| D | TYR187 |
| D | ARG192 |
| D | HIS225 |
| D | ASN226 |
| D | ARG297 |
| D | GLN299 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20106986 |
| Chain | Residue | Details |
| B | GLU81 | |
| B | HIS182 | |
| B | GLU617 | |
| B | SER667 | |
| C | GLU81 | |
| C | HIS182 | |
| C | GLU617 | |
| C | SER667 | |
| D | GLU81 | |
| D | HIS182 | |
| D | GLU617 | |
| D | SER667 | |
| A | GLU81 | |
| A | HIS182 | |
| A | GLU617 | |
| A | SER667 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: |
| Chain | Residue | Details |
| C | TYR160 | |
| C | ARG297 | |
| C | THR703 | |
| C | SER723 | |
| D | TYR160 | |
| D | ARG297 | |
| D | THR703 | |
| D | SER723 | |
| A | TYR160 | |
| A | ARG297 | |
| A | THR703 | |
| A | SER723 | |
| B | TYR160 | |
| B | ARG297 | |
| B | THR703 | |
| B | SER723 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: axial binding residue => ECO:0000269|PubMed:20106986 |
| Chain | Residue | Details |
| A | HIS618 | |
| B | HIS618 | |
| C | HIS618 | |
| D | HIS618 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:20106986 |
| Chain | Residue | Details |
| A | LYS629 | |
| B | LYS629 | |
| C | LYS629 | |
| D | LYS629 |
