2OJP
The crystal structure of a dimeric mutant of Dihydrodipicolinate synthase from E.coli- DHDPS-L197Y
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0008840 | molecular_function | 4-hydroxy-tetrahydrodipicolinate synthase activity |
A | 0009085 | biological_process | lysine biosynthetic process |
A | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
A | 0016829 | molecular_function | lyase activity |
A | 0019877 | biological_process | diaminopimelate biosynthetic process |
A | 0042802 | molecular_function | identical protein binding |
A | 0044281 | biological_process | small molecule metabolic process |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0008840 | molecular_function | 4-hydroxy-tetrahydrodipicolinate synthase activity |
B | 0009085 | biological_process | lysine biosynthetic process |
B | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
B | 0016829 | molecular_function | lyase activity |
B | 0019877 | biological_process | diaminopimelate biosynthetic process |
B | 0042802 | molecular_function | identical protein binding |
B | 0044281 | biological_process | small molecule metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 1001 |
Chain | Residue |
A | SER23 |
A | LYS26 |
A | GLY260 |
A | LEU261 |
A | VAL262 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL B 1002 |
Chain | Residue |
B | HOH1403 |
B | SER23 |
B | LYS26 |
B | GLY260 |
B | ALA263 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor/acceptor |
Chain | Residue | Details |
A | TYR133 | |
B | TYR133 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Schiff-base intermediate with substrate |
Chain | Residue | Details |
A | KGC161 | |
B | KGC161 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00418, ECO:0000269|PubMed:20353808, ECO:0000269|PubMed:22552955 |
Chain | Residue | Details |
A | THR45 | |
A | ILE203 | |
B | THR45 | |
B | ILE203 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Part of a proton relay during catalysis |
Chain | Residue | Details |
A | THR44 | |
A | TYR107 | |
B | THR44 | |
B | TYR107 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | SITE: L-lysine inhibitor binding; via carbonyl oxygen |
Chain | Residue | Details |
A | ALA49 | |
B | ALA49 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | SITE: L-lysine inhibitor binding |
Chain | Residue | Details |
A | ASN80 | |
A | GLU84 | |
A | TYR106 | |
B | ASN80 | |
B | GLU84 | |
B | TYR106 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dhp |
Chain | Residue | Details |
A | ARG138 | |
A | TYR133 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dhp |
Chain | Residue | Details |
B | ARG138 | |
B | TYR133 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dhp |
Chain | Residue | Details |
A | THR44 | |
A | THR45 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dhp |
Chain | Residue | Details |
B | THR44 | |
B | THR45 |
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 267 |
Chain | Residue | Details |
A | THR44 | hydrogen bond acceptor, hydrogen bond donor |
A | TYR107 | hydrogen bond donor |
A | TYR133 | activator, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay |
A | ARG138 | electrostatic stabiliser |
A | KGC161 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
A | ILE203 | activator, increase electrophilicity, polar interaction, steric role |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 267 |
Chain | Residue | Details |
B | THR44 | hydrogen bond acceptor, hydrogen bond donor |
B | TYR107 | hydrogen bond donor |
B | TYR133 | activator, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay |
B | ARG138 | electrostatic stabiliser |
B | KGC161 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
B | ILE203 | activator, increase electrophilicity, polar interaction, steric role |