2DX7
Crystal structure of Pyrococcus horikoshii OT3 aspartate racemase complex with citric acid
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006807 | biological_process | obsolete nitrogen compound metabolic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016855 | molecular_function | racemase and epimerase activity, acting on amino acids and derivatives |
| A | 0036361 | molecular_function | racemase activity, acting on amino acids and derivatives |
| A | 0047661 | molecular_function | amino-acid racemase activity |
| A | 0047689 | molecular_function | aspartate racemase activity |
| B | 0006807 | biological_process | obsolete nitrogen compound metabolic process |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016855 | molecular_function | racemase and epimerase activity, acting on amino acids and derivatives |
| B | 0036361 | molecular_function | racemase activity, acting on amino acids and derivatives |
| B | 0047661 | molecular_function | amino-acid racemase activity |
| B | 0047689 | molecular_function | aspartate racemase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CIT A 501 |
| Chain | Residue |
| A | MET10 |
| A | TYR160 |
| A | LYS164 |
| A | CYS194 |
| A | THR195 |
| A | GLU196 |
| A | HOH507 |
| A | ASP47 |
| A | ARG48 |
| A | THR49 |
| A | ALA82 |
| A | ASN83 |
| A | THR84 |
| A | ALA85 |
| A | THR124 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE CIT A 502 |
| Chain | Residue |
| A | PRO61 |
| A | ILE64 |
| A | GLY115 |
| A | LYS117 |
| A | LYS118 |
| A | GLU188 |
| A | HOH590 |
| A | HOH591 |
| B | THR148 |
| B | GLU149 |
| B | ASP150 |
| B | HOH241 |
| B | HOH309 |
Functional Information from PROSITE/UniProt
| site_id | PS00924 |
| Number of Residues | 11 |
| Details | ASP_GLU_RACEMASE_2 Aspartate and glutamate racemases signature 2. IIaGCTEVSvV |
| Chain | Residue | Details |
| A | ILE190-VAL200 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:17847084 |
| Chain | Residue | Details |
| A | ALA82 | |
| A | CYS194 | |
| B | ALA82 | |
| B | CYS194 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:17847084, ECO:0007744|PDB:2DX7 |
| Chain | Residue | Details |
| A | ASP47 | |
| A | ASN83 | |
| A | LYS164 | |
| B | ASP47 | |
| B | ASN83 | |
| B | LYS164 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 335 |
| Chain | Residue | Details |
| A | ARG48 | electrostatic stabiliser, hydrogen bond donor |
| A | ALA82 | proton acceptor |
| A | THR84 | electrostatic stabiliser, hydrogen bond donor |
| A | THR124 | electrostatic stabiliser, hydrogen bond donor |
| A | LYS164 | electrostatic stabiliser, hydrogen bond donor |
| A | CYS194 | activator, hydrogen bond donor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 335 |
| Chain | Residue | Details |
| B | ARG48 | electrostatic stabiliser, hydrogen bond donor |
| B | ALA82 | proton acceptor |
| B | THR84 | electrostatic stabiliser, hydrogen bond donor |
| B | THR124 | electrostatic stabiliser, hydrogen bond donor |
| B | LYS164 | electrostatic stabiliser, hydrogen bond donor |
| B | CYS194 | activator, hydrogen bond donor, proton donor |
