1HKW
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 | 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 | 0016830 | molecular_function | carbon-carbon 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 | 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 | 0016830 | molecular_function | carbon-carbon 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 | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 500 |
Chain | Residue |
A | GLY258 |
A | PRO301 |
A | GLY302 |
A | ARG303 |
A | TYR405 |
A | HOH2121 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 501 |
Chain | Residue |
B | ARG303 |
B | TYR405 |
B | HOH2093 |
B | GLY258 |
B | PRO301 |
B | GLY302 |
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 |