1NXJ
Structure of Rv3853 from Mycobacterium tuberculosis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008428 | molecular_function | ribonuclease inhibitor activity |
| A | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| A | 0008948 | molecular_function | oxaloacetate decarboxylase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047443 | molecular_function | 4-hydroxy-4-methyl-2-oxoglutarate aldolase activity |
| A | 0051252 | biological_process | regulation of RNA metabolic process |
| B | 0008428 | molecular_function | ribonuclease inhibitor activity |
| B | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| B | 0008948 | molecular_function | oxaloacetate decarboxylase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047443 | molecular_function | 4-hydroxy-4-methyl-2-oxoglutarate aldolase activity |
| B | 0051252 | biological_process | regulation of RNA metabolic process |
| C | 0008428 | molecular_function | ribonuclease inhibitor activity |
| C | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
| C | 0008948 | molecular_function | oxaloacetate decarboxylase activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0047443 | molecular_function | 4-hydroxy-4-methyl-2-oxoglutarate aldolase activity |
| C | 0051252 | biological_process | regulation of RNA metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GLV A 741 |
| Chain | Residue |
| A | GLN25 |
| A | PHE26 |
| A | ARG27 |
| A | THR117 |
| A | ASP151 |
| A | HOH751 |
| A | HOH802 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GLV B 742 |
| Chain | Residue |
| B | PHE26 |
| B | ARG27 |
| B | THR117 |
| B | ASP151 |
| B | HOH755 |
| B | LEU24 |
| B | GLN25 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GLV C 743 |
| Chain | Residue |
| C | GLN25 |
| C | PHE26 |
| C | ARG27 |
| C | THR117 |
| C | ASP151 |
| C | HOH759 |
| C | HOH771 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE TLA A 391 |
| Chain | Residue |
| A | ASN48 |
| A | ALA75 |
| A | GLY78 |
| A | ASP79 |
| A | VAL80 |
| A | ILE81 |
| A | ARG100 |
| A | LYS121 |
| A | SER122 |
| A | LYS124 |
| A | HOH777 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE TLA B 392 |
| Chain | Residue |
| B | ASN48 |
| B | ALA75 |
| B | GLY78 |
| B | ASP79 |
| B | VAL80 |
| B | ILE81 |
| B | ARG100 |
| B | LYS121 |
| B | SER122 |
| B | LYS124 |
| B | HOH777 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE TLA C 393 |
| Chain | Residue |
| C | ASN48 |
| C | ALA75 |
| C | GLY78 |
| C | ASP79 |
| C | VAL80 |
| C | ILE81 |
| C | ARG100 |
| C | LYS121 |
| C | SER122 |
| C | LYS124 |
| C | HOH821 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 9 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLY78 | |
| A | ARG100 | |
| A | ASP101 | |
| B | GLY78 | |
| B | ARG100 | |
| B | ASP101 | |
| C | GLY78 | |
| C | ARG100 | |
| C | ASP101 |
