1TZ2
Crystal structure of 1-aminocyclopropane-1-carboyxlate deaminase complexed with ACC
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 | 0018871 | biological_process | 1-aminocyclopropane-1-carboxylate metabolic process |
A | 0019148 | molecular_function | D-cysteine desulfhydrase 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 | 0018871 | biological_process | 1-aminocyclopropane-1-carboxylate metabolic process |
B | 0019148 | molecular_function | D-cysteine desulfhydrase 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 | 0018871 | biological_process | 1-aminocyclopropane-1-carboxylate metabolic process |
C | 0019148 | molecular_function | D-cysteine desulfhydrase 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 | 0018871 | biological_process | 1-aminocyclopropane-1-carboxylate metabolic process |
D | 0019148 | molecular_function | D-cysteine desulfhydrase activity |
D | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE PLP A 401 |
Chain | Residue |
A | ASN50 |
A | GLY200 |
A | SER201 |
A | THR202 |
A | TYR294 |
A | GLU295 |
A | LEU322 |
A | GLY323 |
A | GLY324 |
A | 1AC501 |
A | HOH516 |
A | LYS51 |
A | HOH530 |
A | LYS54 |
A | ASN79 |
A | SER163 |
A | CYS196 |
A | SER197 |
A | VAL198 |
A | THR199 |
site_id | AC2 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE PLP B 401 |
Chain | Residue |
B | ASN50 |
B | LYS51 |
B | LYS54 |
B | ASN79 |
B | SER163 |
B | CYS196 |
B | SER197 |
B | VAL198 |
B | THR199 |
B | GLY200 |
B | THR202 |
B | TYR294 |
B | GLU295 |
B | LEU322 |
B | GLY323 |
B | GLY324 |
B | 1AC501 |
B | HOH509 |
B | HOH535 |
site_id | AC3 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE PLP C 401 |
Chain | Residue |
C | ASN50 |
C | LYS51 |
C | LYS54 |
C | ASN79 |
C | CYS196 |
C | SER197 |
C | VAL198 |
C | THR199 |
C | GLY200 |
C | SER201 |
C | THR202 |
C | TYR294 |
C | GLU295 |
C | LEU322 |
C | GLY323 |
C | GLY324 |
C | 1AC501 |
C | HOH512 |
C | HOH523 |
site_id | AC4 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE PLP D 401 |
Chain | Residue |
D | ASN50 |
D | LYS51 |
D | LYS54 |
D | ASN79 |
D | CYS196 |
D | SER197 |
D | VAL198 |
D | THR199 |
D | GLY200 |
D | SER201 |
D | THR202 |
D | TYR294 |
D | GLU295 |
D | LEU322 |
D | GLY323 |
D | GLY324 |
D | 1AC501 |
D | HOH529 |
D | HOH539 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE 1AC A 501 |
Chain | Residue |
A | LYS51 |
A | SER78 |
A | ASN79 |
A | GLN80 |
A | GLY161 |
A | THR199 |
A | TYR294 |
A | PLP401 |
A | HOH504 |
A | HOH535 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE 1AC B 501 |
Chain | Residue |
B | LYS51 |
B | SER78 |
B | ASN79 |
B | GLN80 |
B | GLY161 |
B | THR199 |
B | TYR294 |
B | PLP401 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE 1AC C 501 |
Chain | Residue |
C | GLY161 |
C | THR199 |
C | TYR294 |
C | PLP401 |
C | LYS51 |
C | SER78 |
C | ASN79 |
C | GLN80 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 1AC D 501 |
Chain | Residue |
D | LYS51 |
D | SER78 |
D | ASN79 |
D | GLN80 |
D | GLY161 |
D | THR199 |
D | TYR294 |
D | PLP401 |
D | HOH582 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00807 |
Chain | Residue | Details |
A | SER78 | |
B | SER78 | |
C | SER78 | |
D | SER78 |
site_id | SWS_FT_FI2 |
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 | TYR294 | |
A | SER78 | |
A | GLU295 |
site_id | CSA2 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1f2d |
Chain | Residue | Details |
B | THR81 | |
B | LYS51 | |
B | TYR294 | |
B | SER78 | |
B | GLU295 |
site_id | CSA3 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1f2d |
Chain | Residue | Details |
C | THR81 | |
C | LYS51 | |
C | TYR294 | |
C | SER78 | |
C | GLU295 |
site_id | CSA4 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1f2d |
Chain | Residue | Details |
D | THR81 | |
D | LYS51 | |
D | TYR294 | |
D | SER78 | |
D | GLU295 |
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 |