3KP1
Crystal structure of ornithine 4,5 aminomutase (Resting State)
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 | 13 |
| Details | BINDING SITE FOR RESIDUE PLP A 1802 |
| Chain | Residue |
| A | LYS629 |
| C | ARG192 |
| C | HIS225 |
| C | ASN226 |
| C | HOH908 |
| A | HOH1661 |
| C | ARG109 |
| C | GLY112 |
| C | GLN113 |
| C | SER114 |
| C | TYR160 |
| C | SER162 |
| C | TYR187 |
| site_id | AC2 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE B12 A 1801 |
| Chain | Residue |
| A | GLU617 |
| A | HIS618 |
| A | SER619 |
| A | VAL620 |
| A | GLY621 |
| A | VAL625 |
| A | ALA666 |
| A | SER667 |
| A | ILE669 |
| A | ILE670 |
| A | SER671 |
| A | HIS672 |
| A | GLY701 |
| A | GLY702 |
| A | THR703 |
| A | PHE719 |
| A | GLY720 |
| A | SER723 |
| A | VAL728 |
| A | HOH912 |
| A | HOH950 |
| A | HOH1297 |
| A | HOH2153 |
| A | HOH2982 |
| C | HIS115 |
| C | TYR116 |
| C | ILE127 |
| C | 5AD767 |
| C | HOH1285 |
| C | HOH2766 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE 5AD A 767 |
| Chain | Residue |
| A | LEU489 |
| A | HOH861 |
| A | HOH923 |
| A | HOH1074 |
| C | B121801 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP B 1802 |
| Chain | Residue |
| B | LYS629 |
| B | HIS630 |
| B | HOH774 |
| B | HOH967 |
| D | ARG109 |
| D | GLY112 |
| D | GLN113 |
| D | SER114 |
| D | TYR160 |
| D | SER162 |
| D | TYR187 |
| D | ARG192 |
| D | HIS225 |
| D | ASN226 |
| site_id | AC5 |
| Number of Residues | 40 |
| Details | BINDING SITE FOR RESIDUE B12 B 1801 |
| Chain | Residue |
| D | HOH856 |
| D | HOH936 |
| D | HOH1594 |
| B | GLU615 |
| B | GLU617 |
| B | HIS618 |
| B | SER619 |
| B | VAL620 |
| B | GLY621 |
| B | VAL625 |
| 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 |
| B | HOH807 |
| B | HOH850 |
| B | HOH858 |
| B | HOH943 |
| B | HOH956 |
| B | HOH1004 |
| B | HOH1232 |
| B | HOH1883 |
| B | HOH1978 |
| B | HOH2337 |
| B | HOH2813 |
| B | HOH2819 |
| B | HOH3190 |
| D | HIS115 |
| D | TYR116 |
| D | ASP490 |
| D | 5AD767 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE 5AD B 767 |
| Chain | Residue |
| B | LEU489 |
| B | HOH781 |
| B | HOH983 |
| B | HOH1019 |
| D | B121801 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP D 1802 |
| Chain | Residue |
| B | ARG109 |
| B | GLY112 |
| B | GLN113 |
| B | SER114 |
| B | TYR160 |
| B | SER162 |
| B | TYR187 |
| B | ARG192 |
| B | HIS225 |
| B | ASN226 |
| D | LYS629 |
| D | HOH823 |
| D | HOH844 |
| site_id | AC8 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE B12 D 1801 |
| Chain | Residue |
| B | TYR116 |
| B | ILE127 |
| B | 5AD767 |
| B | HOH781 |
| B | HOH860 |
| B | HOH1534 |
| B | HOH3091 |
| D | GLU615 |
| D | GLU617 |
| D | HIS618 |
| D | SER619 |
| D | VAL620 |
| D | GLY621 |
| 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 | SER723 |
| D | VAL728 |
| D | HOH875 |
| D | HOH886 |
| D | HOH975 |
| D | HOH1504 |
| D | HOH1759 |
| D | HOH1921 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 5AD D 767 |
| Chain | Residue |
| B | B121801 |
| D | LEU489 |
| D | HOH785 |
| D | HOH915 |
| D | HOH990 |
| D | HOH1020 |
| D | HOH2785 |
| site_id | BC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP C 1802 |
| Chain | Residue |
| A | ARG109 |
| A | GLY112 |
| A | GLN113 |
| A | SER114 |
| A | TYR160 |
| A | SER162 |
| A | TYR187 |
| A | ARG192 |
| A | HIS225 |
| A | ASN226 |
| A | HOH1618 |
| C | LYS629 |
| C | HOH854 |
| C | HOH874 |
| site_id | BC2 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE B12 C 1801 |
| Chain | Residue |
| A | TYR116 |
| A | ILE127 |
| A | 5AD767 |
| A | HOH923 |
| A | HOH1045 |
| C | GLU615 |
| C | GLU617 |
| C | HIS618 |
| C | SER619 |
| C | VAL620 |
| C | GLY621 |
| C | GLU624 |
| C | VAL625 |
| C | ALA666 |
| C | SER667 |
| C | ILE669 |
| C | ILE670 |
| C | SER671 |
| C | HIS672 |
| C | GLY701 |
| C | GLY702 |
| C | THR703 |
| C | PHE719 |
| C | GLY720 |
| C | SER723 |
| C | VAL728 |
| C | HOH782 |
| C | HOH787 |
| C | HOH843 |
| C | HOH946 |
| C | HOH952 |
| C | HOH984 |
| C | HOH989 |
| C | HOH1036 |
| C | HOH1251 |
| C | HOH1362 |
| C | HOH1706 |
| C | HOH1779 |
| C | HOH2998 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 5AD C 767 |
| Chain | Residue |
| A | B121801 |
| C | LEU489 |
| C | HOH936 |
| C | HOH1063 |
| C | HOH1699 |
| C | HOH2858 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20106986","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| 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 | 4 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"20106986","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
