3C3D
Crystal structure of 2-phospho-(S)-lactate transferase from Methanosarcina mazei in complex with Fo and phosphate. Northeast Structural Genomics Consortium target MaR46
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| A | 0043743 | molecular_function | LPPG:FO 2-phospho-L-lactate transferase activity |
| A | 0052645 | biological_process | F420-0 metabolic process |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| B | 0043743 | molecular_function | LPPG:FO 2-phospho-L-lactate transferase activity |
| B | 0052645 | biological_process | F420-0 metabolic process |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| C | 0043743 | molecular_function | LPPG:FO 2-phospho-L-lactate transferase activity |
| C | 0052645 | biological_process | F420-0 metabolic process |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| D | 0043743 | molecular_function | LPPG:FO 2-phospho-L-lactate transferase activity |
| D | 0052645 | biological_process | F420-0 metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 A 402 |
| Chain | Residue |
| A | GLY7 |
| A | THR8 |
| A | SER192 |
| A | ASN193 |
| A | SER197 |
| A | SER229 |
| A | HOH476 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 402 |
| Chain | Residue |
| B | SER192 |
| B | ASN193 |
| B | SER197 |
| B | HOH443 |
| B | GLY7 |
| B | THR8 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 C 402 |
| Chain | Residue |
| C | GLY7 |
| C | THR8 |
| C | SER192 |
| C | ASN193 |
| C | SER197 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 D 402 |
| Chain | Residue |
| D | GLY7 |
| D | THR8 |
| D | SER192 |
| D | ASN193 |
| D | SER197 |
| D | SER229 |
| D | HOH405 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FO1 A 401 |
| Chain | Residue |
| A | PRO45 |
| A | TRP64 |
| A | LYS87 |
| A | ASP92 |
| A | TRP151 |
| A | HOH452 |
| A | HOH481 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FO1 B 401 |
| Chain | Residue |
| B | PRO45 |
| B | TRP64 |
| B | LYS87 |
| B | ASP92 |
| B | HOH407 |
| B | HOH445 |
| B | HOH447 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FO1 C 401 |
| Chain | Residue |
| C | PRO45 |
| C | TRP64 |
| C | LYS87 |
| C | ASP92 |
| C | HOH407 |
| C | HOH429 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FO1 D 401 |
| Chain | Residue |
| D | PRO45 |
| D | TRP64 |
| D | LEU86 |
| D | LYS87 |
| D | ASP92 |
| D | TRP151 |
| D | ILE152 |
| D | HOH404 |
| D | HOH480 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18252724 |
| Chain | Residue | Details |
| A | ASP48 | |
| A | LYS87 | |
| B | ASP48 | |
| B | LYS87 | |
| C | ASP48 | |
| C | LYS87 | |
| D | ASP48 | |
| D | LYS87 |
