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 | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20106986 |
Chain | Residue | Details |
A | GLU81 | |
C | HIS182 | |
C | GLU617 | |
C | SER667 | |
D | GLU81 | |
D | HIS182 | |
D | GLU617 | |
D | SER667 | |
A | HIS182 | |
A | GLU617 | |
A | SER667 | |
B | GLU81 | |
B | HIS182 | |
B | GLU617 | |
B | SER667 | |
C | GLU81 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: |
Chain | Residue | Details |
A | TYR160 | |
C | ARG297 | |
C | THR703 | |
C | SER723 | |
D | TYR160 | |
D | ARG297 | |
D | THR703 | |
D | SER723 | |
A | ARG297 | |
A | THR703 | |
A | SER723 | |
B | TYR160 | |
B | ARG297 | |
B | THR703 | |
B | SER723 | |
C | TYR160 |
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 |