1J0E
ACC deaminase mutant reacton intermediate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008660 | molecular_function | 1-aminocyclopropane-1-carboxylate deaminase activity |
A | 0009310 | biological_process | amine catabolic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0008660 | molecular_function | 1-aminocyclopropane-1-carboxylate deaminase activity |
B | 0009310 | biological_process | amine catabolic process |
B | 0016787 | molecular_function | hydrolase activity |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
C | 0008660 | molecular_function | 1-aminocyclopropane-1-carboxylate deaminase activity |
C | 0009310 | biological_process | amine catabolic process |
C | 0016787 | molecular_function | hydrolase activity |
C | 0030170 | molecular_function | pyridoxal phosphate binding |
D | 0008660 | molecular_function | 1-aminocyclopropane-1-carboxylate deaminase activity |
D | 0009310 | biological_process | amine catabolic process |
D | 0016787 | molecular_function | hydrolase activity |
D | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE PLP A 1401 |
Chain | Residue |
A | ASN50 |
A | SER204 |
A | THR205 |
A | PHE295 |
A | GLU296 |
A | GLY324 |
A | 1AC1001 |
A | HOH1468 |
A | HOH1479 |
A | LYS51 |
A | LYS54 |
A | ASN79 |
A | SER166 |
A | CYS199 |
A | VAL201 |
A | THR202 |
A | GLY203 |
site_id | AC2 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE PLP B 1501 |
Chain | Residue |
B | ASN50 |
B | LYS51 |
B | LYS54 |
B | ASN79 |
B | CYS199 |
B | CYS200 |
B | VAL201 |
B | THR202 |
B | GLY203 |
B | SER204 |
B | THR205 |
B | PHE295 |
B | GLU296 |
B | LEU323 |
B | GLY324 |
B | GLY325 |
B | 1AC2001 |
B | HOH2006 |
B | HOH2071 |
site_id | AC3 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE PLP C 1601 |
Chain | Residue |
C | ASN50 |
C | LYS51 |
C | LYS54 |
C | ASN79 |
C | SER166 |
C | VAL201 |
C | THR202 |
C | GLY203 |
C | THR205 |
C | PHE295 |
C | GLU296 |
C | LEU323 |
C | GLY324 |
C | GLY325 |
C | 1AC3001 |
C | HOH3139 |
C | HOH3373 |
site_id | AC4 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE PLP D 1701 |
Chain | Residue |
D | ASN50 |
D | LYS51 |
D | LYS54 |
D | ASN79 |
D | VAL201 |
D | THR202 |
D | GLY203 |
D | SER204 |
D | THR205 |
D | PHE295 |
D | GLU296 |
D | LEU323 |
D | GLY324 |
D | GLY325 |
D | 1AC4001 |
D | HOH4011 |
D | HOH4115 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE 1AC A 1001 |
Chain | Residue |
A | LYS51 |
A | SER78 |
A | ASN79 |
A | GLN80 |
A | PHE295 |
A | PLP1401 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE 1AC B 2001 |
Chain | Residue |
B | LYS51 |
B | SER78 |
B | ASN79 |
B | GLN80 |
B | PHE295 |
B | PLP1501 |
B | HOH2124 |
B | HOH2125 |
site_id | AC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE 1AC C 3001 |
Chain | Residue |
C | LYS51 |
C | SER78 |
C | ASN79 |
C | GLN80 |
C | TRP102 |
C | PHE295 |
C | PLP1601 |
C | HOH3003 |
C | HOH3011 |
C | HOH3373 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 1AC D 4001 |
Chain | Residue |
D | PHE295 |
D | PLP1701 |
D | HOH4031 |
D | HOH4061 |
D | LYS51 |
D | SER78 |
D | ASN79 |
D | GLN80 |
D | TRP102 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Nucleophile |
Chain | Residue | Details |
A | SER78 | |
B | SER78 | |
C | SER78 | |
D | SER78 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | MOD_RES: N-acetylserine => ECO:0000269|PubMed:9604000 |
Chain | Residue | Details |
A | ALA1 | |
B | ALA1 | |
C | ALA1 | |
D | ALA1 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine |
Chain | Residue | Details |
A | LYS51 | |
B | LYS51 | |
C | LYS51 | |
D | LYS51 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1f2d |
Chain | Residue | Details |
A | THR81 | |
A | LYS51 | |
A | GLU296 | |
A | SER78 | |
A | PHE295 |
site_id | CSA2 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1f2d |
Chain | Residue | Details |
B | THR81 | |
B | LYS51 | |
B | GLU296 | |
B | SER78 | |
B | PHE295 |
site_id | CSA3 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1f2d |
Chain | Residue | Details |
C | THR81 | |
C | LYS51 | |
C | GLU296 | |
C | SER78 | |
C | PHE295 |
site_id | CSA4 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1f2d |
Chain | Residue | Details |
D | THR81 | |
D | LYS51 | |
D | GLU296 | |
D | SER78 | |
D | PHE295 |
site_id | CSA5 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1f2d |
Chain | Residue | Details |
A | LYS51 |
site_id | CSA6 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1f2d |
Chain | Residue | Details |
B | LYS51 |
site_id | CSA7 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1f2d |
Chain | Residue | Details |
C | LYS51 |
site_id | CSA8 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1f2d |
Chain | Residue | Details |
D | LYS51 |
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 545 |
Chain | Residue | Details |
A | LYS51 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |
A | TYR269 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile |
A | PHE295 | electrostatic stabiliser, proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 545 |
Chain | Residue | Details |
B | LYS51 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |
B | TYR269 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile |
B | PHE295 | electrostatic stabiliser, proton acceptor, proton donor |
site_id | MCSA3 |
Number of Residues | 3 |
Details | M-CSA 545 |
Chain | Residue | Details |
C | LYS51 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |
C | TYR269 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile |
C | PHE295 | electrostatic stabiliser, proton acceptor, proton donor |
site_id | MCSA4 |
Number of Residues | 3 |
Details | M-CSA 545 |
Chain | Residue | Details |
D | LYS51 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |
D | TYR269 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile |
D | PHE295 | electrostatic stabiliser, proton acceptor, proton donor |