1HKV
mycobacterium diaminopimelate dicarboxylase (lysa)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0008836 | molecular_function | diaminopimelate decarboxylase activity |
| A | 0009085 | biological_process | lysine biosynthetic process |
| A | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| A | 0009274 | cellular_component | peptidoglycan-based cell wall |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0008836 | molecular_function | diaminopimelate decarboxylase activity |
| B | 0009085 | biological_process | lysine biosynthetic process |
| B | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| B | 0009274 | cellular_component | peptidoglycan-based cell wall |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE LYS A 501 |
| Chain | Residue |
| A | LYS72 |
| A | SER216 |
| A | ARG303 |
| A | ARG344 |
| B | GLU376 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE LYS B 501 |
| Chain | Residue |
| B | HIS213 |
| B | SER216 |
| B | ARG303 |
| B | TYR348 |
| B | TYR405 |
| A | GLU376 |
| A | SER377 |
| A | TYR413 |
| B | LYS72 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP A 500 |
| Chain | Residue |
| A | ALA70 |
| A | LYS72 |
| A | ARG161 |
| A | HIS213 |
| A | GLY257 |
| A | GLY258 |
| A | GLU300 |
| A | GLY302 |
| A | ARG303 |
| A | TYR405 |
| A | HOH2064 |
| A | HOH2109 |
| B | CYS375 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP B 500 |
| Chain | Residue |
| A | CYS375 |
| B | LYS72 |
| B | HIS213 |
| B | SER216 |
| B | GLY257 |
| B | GLY258 |
| B | GLU300 |
| B | GLY302 |
| B | ARG303 |
| B | TYR405 |
| B | HOH2126 |
| B | HOH2127 |
Functional Information from PROSITE/UniProt
| site_id | PS00878 |
| Number of Residues | 19 |
| Details | ODR_DC_2_1 Orn/DAP/Arg decarboxylases family 2 pyridoxal-P attachment site. YAaKAFlcseVArwIseeG |
| Chain | Residue | Details |
| A | TYR69-GLY87 |
| site_id | PS00879 |
| Number of Residues | 18 |
| Details | ODR_DC_2_2 Orn/DAP/Arg decarboxylases family 2 signature 2. GpektaqIaTVDLGGGLG |
| Chain | Residue | Details |
| A | GLY243-GLY260 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_02120 |
| Chain | Residue | Details |
| A | CYS375 | |
| B | CYS375 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:12637582 |
| Chain | Residue | Details |
| A | SER216 | |
| B | TYR405 | |
| A | ARG303 | |
| A | ARG344 | |
| A | GLU376 | |
| A | TYR405 | |
| B | SER216 | |
| B | ARG303 | |
| B | ARG344 | |
| B | GLU376 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12637582 |
| Chain | Residue | Details |
| A | GLY258 | |
| B | GLY258 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02120, ECO:0000269|PubMed:12637582 |
| Chain | Residue | Details |
| A | GLU300 | |
| B | GLU300 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02120 |
| Chain | Residue | Details |
| A | TYR348 | |
| B | TYR348 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:12637582 |
| Chain | Residue | Details |
| A | LYS72 | |
| B | LYS72 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1bd0 |
| Chain | Residue | Details |
| A | LYS182 | |
| A | LYS72 | |
| B | CYS375 | |
| B | HIS329 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1bd0 |
| Chain | Residue | Details |
| A | CYS375 | |
| A | HIS329 | |
| B | LYS182 | |
| B | LYS72 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bd0 |
| Chain | Residue | Details |
| A | GLU300 | |
| A | HIS213 | |
| A | LYS72 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bd0 |
| Chain | Residue | Details |
| B | GLU300 | |
| B | HIS213 | |
| B | LYS72 |
