6BWH
Crystal structure of Mycoibacterium tuberculosis Rv2983 in complex with PEP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005525 | molecular_function | GTP binding |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0043814 | molecular_function | phospholactate guanylyltransferase activity |
| A | 0052645 | biological_process | F420-0 metabolic process |
| A | 0070568 | molecular_function | guanylyltransferase activity |
| B | 0005525 | molecular_function | GTP binding |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0043814 | molecular_function | phospholactate guanylyltransferase activity |
| B | 0052645 | biological_process | F420-0 metabolic process |
| B | 0070568 | molecular_function | guanylyltransferase activity |
| C | 0005525 | molecular_function | GTP binding |
| C | 0016779 | molecular_function | nucleotidyltransferase activity |
| C | 0043814 | molecular_function | phospholactate guanylyltransferase activity |
| C | 0052645 | biological_process | F420-0 metabolic process |
| C | 0070568 | molecular_function | guanylyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue PEP A 301 |
| Chain | Residue |
| A | LEU92 |
| A | MG302 |
| A | MG303 |
| A | HOH403 |
| A | HOH421 |
| A | HOH422 |
| A | HOH432 |
| A | GLN114 |
| A | GLY147 |
| A | THR148 |
| A | PHE162 |
| A | GLY163 |
| A | SER166 |
| A | ASP188 |
| A | ASP190 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue MG A 302 |
| Chain | Residue |
| A | ASP142 |
| A | ASP188 |
| A | ASP190 |
| A | PEP301 |
| A | MG303 |
| A | HOH421 |
| A | HOH422 |
| A | HOH428 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue MG A 303 |
| Chain | Residue |
| A | ASP116 |
| A | ASP188 |
| A | ASP190 |
| A | PEP301 |
| A | MG302 |
| A | HOH403 |
| A | HOH417 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | binding site for residue PEP B 301 |
| Chain | Residue |
| B | LYS17 |
| B | LEU92 |
| B | GLN114 |
| B | GLY147 |
| B | THR148 |
| B | PHE162 |
| B | GLY163 |
| B | SER166 |
| B | ASP188 |
| B | ASP190 |
| B | MG302 |
| B | MG303 |
| B | HOH401 |
| B | HOH404 |
| B | HOH410 |
| B | HOH417 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue MG B 302 |
| Chain | Residue |
| B | ASP188 |
| B | ASP190 |
| B | PEP301 |
| B | MG303 |
| B | HOH401 |
| B | HOH417 |
| B | HOH431 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue MG B 303 |
| Chain | Residue |
| B | ASP116 |
| B | ASP188 |
| B | ASP190 |
| B | PEP301 |
| B | MG302 |
| B | HOH410 |
| B | HOH415 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | binding site for residue PEP C 301 |
| Chain | Residue |
| C | LEU92 |
| C | GLN114 |
| C | GLY147 |
| C | THR148 |
| C | PHE162 |
| C | GLY163 |
| C | SER166 |
| C | ASP188 |
| C | ASP190 |
| C | MG302 |
| C | MG303 |
| C | HOH401 |
| C | HOH402 |
| C | HOH412 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue MG C 302 |
| Chain | Residue |
| C | ASP188 |
| C | ASP190 |
| C | PEP301 |
| C | MG303 |
| C | HOH401 |
| C | HOH408 |
| C | HOH412 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue MG C 303 |
| Chain | Residue |
| C | ASP116 |
| C | ASP188 |
| C | ASP190 |
| C | PEP301 |
| C | MG302 |
| C | HOH402 |
| C | HOH404 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 9 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:30952857 |
| Chain | Residue | Details |
| A | THR148 | |
| A | GLY163 | |
| A | SER166 | |
| B | THR148 | |
| B | GLY163 | |
| B | SER166 | |
| C | THR148 | |
| C | GLY163 | |
| C | SER166 |
