3B7W
Crystal structure of human acyl-CoA synthetase medium-chain family member 2A, with L64P mutation
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004321 | molecular_function | fatty-acyl-CoA synthase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0006637 | biological_process | acyl-CoA metabolic process |
| A | 0015645 | molecular_function | fatty acid ligase activity |
| A | 0016405 | molecular_function | CoA-ligase activity |
| A | 0016874 | molecular_function | ligase activity |
| A | 0016878 | molecular_function | acid-thiol ligase activity |
| A | 0018858 | molecular_function | benzoate-CoA ligase activity |
| A | 0031956 | molecular_function | medium-chain fatty acid-CoA ligase activity |
| A | 0036112 | biological_process | medium-chain fatty-acyl-CoA metabolic process |
| A | 0042593 | biological_process | glucose homeostasis |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047760 | molecular_function | butyrate-CoA ligase activity |
| A | 0070328 | biological_process | triglyceride homeostasis |
| A | 0102391 | molecular_function | decanoate-CoA ligase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 601 |
| Chain | Residue |
| A | MET483 |
| A | HIS485 |
| A | VAL488 |
| A | HOH1087 |
| A | HOH1093 |
| A | HOH1094 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 602 |
| Chain | Residue |
| A | ARG472 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 603 |
| Chain | Residue |
| A | THR345 |
| A | ASN348 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 604 |
| Chain | Residue |
| A | GLN352 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 605 |
| Chain | Residue |
| A | SER301 |
| A | SER302 |
| A | HOH830 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 606 |
| Chain | Residue |
| A | SER301 |
| A | SER302 |
| A | TYR303 |
| A | PRO304 |
| A | GLY399 |
| A | ASN400 |
| A | VAL401 |
| A | ARG413 |
| A | ASP440 |
| A | HOH989 |
Functional Information from PROSITE/UniProt
| site_id | PS00455 |
| Number of Residues | 12 |
| Details | AMP_BINDING Putative AMP-binding domain signature. IYFTSGTSGlPK |
| Chain | Residue | Details |
| A | ILE218-LYS229 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 7 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19345228 |
| Chain | Residue | Details |
| A | GLN139 | |
| A | THR364 | |
| A | SER469 | |
| A | ARG472 | |
| A | ARG501 | |
| A | LYS532 | |
| A | TYR540 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19345228, ECO:0000269|Ref.7 |
| Chain | Residue | Details |
| A | THR221 | |
| A | GLU359 | |
| A | ASP446 | |
| A | ARG461 | |
| A | LYS557 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q68CK6 |
| Chain | Residue | Details |
| A | SER513 |
