1V25
Crystal structure of tt0168 from Thermus thermophilus HB8
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0001676 | biological_process | long-chain fatty acid metabolic process |
| A | 0004467 | molecular_function | long-chain fatty acid-CoA ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0016874 | molecular_function | ligase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0001676 | biological_process | long-chain fatty acid metabolic process |
| B | 0004467 | molecular_function | long-chain fatty acid-CoA ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0016874 | molecular_function | ligase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 1001 |
| Chain | Residue |
| A | THR184 |
| A | GLU328 |
| A | ANP666 |
| A | HOH1120 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 1002 |
| Chain | Residue |
| B | THR184 |
| B | GLU328 |
| B | ANP1666 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE ANP A 666 |
| Chain | Residue |
| A | VAL231 |
| A | TRP234 |
| A | GLY302 |
| A | SER303 |
| A | ALA304 |
| A | GLN322 |
| A | GLY323 |
| A | TYR324 |
| A | GLY325 |
| A | LEU326 |
| A | THR327 |
| A | ASP418 |
| A | ARG433 |
| A | LYS435 |
| A | LYS439 |
| A | TRP444 |
| A | MG1001 |
| A | HOH1034 |
| A | HOH1098 |
| A | HOH1191 |
| A | HOH1196 |
| A | HOH1226 |
| A | PHE229 |
| A | HIS230 |
| site_id | AC4 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE ANP B 1666 |
| Chain | Residue |
| B | PHE229 |
| B | HIS230 |
| B | VAL231 |
| B | TRP234 |
| B | GLY302 |
| B | SER303 |
| B | ALA304 |
| B | GLN322 |
| B | GLY323 |
| B | TYR324 |
| B | GLY325 |
| B | LEU326 |
| B | THR327 |
| B | ASP418 |
| B | ARG433 |
| B | LYS435 |
| B | LYS439 |
| B | TRP444 |
| B | MG1002 |
| B | HOH1725 |
| B | HOH1733 |
| B | HOH1734 |
| B | HOH1739 |
| B | HOH1787 |
| B | HOH1801 |
| B | HOH1859 |
Functional Information from PROSITE/UniProt
| site_id | PS00455 |
| Number of Residues | 12 |
| Details | AMP_BINDING Putative AMP-binding domain signature. MAYTTGTTGlPK |
| Chain | Residue | Details |
| A | MET181-LYS192 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15145952, ECO:0007744|PDB:1V25 |
| Chain | Residue | Details |
| A | THR184 | |
| A | GLU328 | |
| B | THR184 | |
| B | GLU328 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:15145952, ECO:0007744|PDB:1V25 |
| Chain | Residue | Details |
| A | VAL231 | |
| A | TRP234 | |
| A | TRP444 | |
| B | VAL231 | |
| B | TRP234 | |
| B | TRP444 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15145952, ECO:0007744|PDB:1V26 |
| Chain | Residue | Details |
| A | GLY302 | |
| B | GLY323 | |
| B | THR327 | |
| B | ASP418 | |
| B | LYS435 | |
| B | LYS439 | |
| A | GLN322 | |
| A | GLY323 | |
| A | THR327 | |
| A | ASP418 | |
| A | LYS435 | |
| A | LYS439 | |
| B | GLY302 | |
| B | GLN322 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 15145952 |
| Chain | Residue | Details |
| A | LYS439 | |
| A | TRP444 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 15145952 |
| Chain | Residue | Details |
| B | LYS439 | |
| B | TRP444 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 198 |
| Chain | Residue | Details |
| A | THR184 | metal ligand |
| A | GLU328 | metal ligand |
| A | LYS439 | electrostatic stabiliser, hydrogen bond donor |
| A | TRP444 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 198 |
| Chain | Residue | Details |
| B | THR184 | metal ligand |
| B | GLU328 | metal ligand |
| B | LYS439 | electrostatic stabiliser, hydrogen bond donor |
| B | TRP444 | electrostatic stabiliser, hydrogen bond donor |
