1GQZ
Refinement of Haemophilus influenzae Diaminopimelate epimerase at 1.7A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008837 | molecular_function | diaminopimelate epimerase activity |
| A | 0009085 | biological_process | lysine biosynthetic process |
| A | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| A | 0016853 | molecular_function | isomerase activity |
Functional Information from PROSITE/UniProt
| site_id | PS01326 |
| Number of Residues | 15 |
| Details | DAP_EPIMERASE Diaminopimelate epimerase signature. NaDGSevsqCGNGaR |
| Chain | Residue | Details |
| A | ASN64-ARG78 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:16723397, ECO:0000305|PubMed:9843410, ECO:0000305|DOI:10.1021/ja001193t, ECO:0007744|PDB:1BWZ, ECO:0007744|PDB:2GKE, ECO:0007744|PDB:2GKJ |
| Chain | Residue | Details |
| A | CYS73 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:16723397, ECO:0000305|PubMed:9843410, ECO:0000305|DOI:10.1021/ja001193t, ECO:0007744|PDB:1BWZ, ECO:0007744|PDB:2GKE, ECO:0007744|PDB:2GKJ |
| Chain | Residue | Details |
| A | CYS217 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16723397, ECO:0007744|PDB:2GKE, ECO:0007744|PDB:2GKJ |
| Chain | Residue | Details |
| A | ASN11 | |
| A | ASN64 | |
| A | GLY74 | |
| A | ASN157 | |
| A | ASN190 | |
| A | GLU208 | |
| A | GLY218 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16723397, ECO:0007744|PDB:2GKJ |
| Chain | Residue | Details |
| A | GLN44 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | SITE: Could be important to modulate the pK values of the two catalytic cysteine residues => ECO:0000305|PubMed:9843410, ECO:0007744|PDB:1BWZ |
| Chain | Residue | Details |
| A | HIS159 | |
| A | GLU208 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | SITE: Important for dimerization => ECO:0000250|UniProtKB:P0A6K1 |
| Chain | Residue | Details |
| A | TYR268 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1bwz |
| Chain | Residue | Details |
| A | GLU208 | |
| A | CYS73 | |
| A | CYS217 | |
| A | HIS159 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 334 |
| Chain | Residue | Details |
| A | CYS73 | hydrogen bond acceptor, proton acceptor |
| A | HIS159 | activator, electrostatic stabiliser |
| A | GLU208 | activator, electrostatic stabiliser |
| A | CYS217 | hydrogen bond donor, proton donor |
| A | GLY220 | electrostatic stabiliser, hydrogen bond donor |
