3EQ6
Crystal structure of human acyl-CoA synthetase medium-chain family member 2A (L64P mutation) in a ternary complex with products
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 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 | 0070328 | biological_process | triglyceride homeostasis |
A | 0102391 | molecular_function | decanoate-CoA ligase activity |
B | 0004321 | molecular_function | fatty-acyl-CoA synthase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005739 | cellular_component | mitochondrion |
B | 0005759 | cellular_component | mitochondrial matrix |
B | 0006631 | biological_process | fatty acid metabolic process |
B | 0006633 | biological_process | fatty acid biosynthetic process |
B | 0006637 | biological_process | acyl-CoA metabolic process |
B | 0015645 | molecular_function | fatty acid ligase activity |
B | 0016405 | molecular_function | CoA-ligase activity |
B | 0016874 | molecular_function | ligase activity |
B | 0016878 | molecular_function | acid-thiol ligase activity |
B | 0018858 | molecular_function | benzoate-CoA ligase activity |
B | 0031956 | molecular_function | medium-chain fatty acid-CoA ligase activity |
B | 0036112 | biological_process | medium-chain fatty-acyl-CoA metabolic process |
B | 0042593 | biological_process | glucose homeostasis |
B | 0046872 | molecular_function | metal ion binding |
B | 0070328 | biological_process | triglyceride homeostasis |
B | 0102391 | molecular_function | decanoate-CoA ligase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE AMP A 901 |
Chain | Residue |
A | GLY338 |
A | ASP446 |
A | PHE458 |
A | ARG461 |
A | ARG472 |
A | BCO911 |
A | HOH1111 |
A | HOH1113 |
A | GLU339 |
A | SER340 |
A | GLU359 |
A | SER360 |
A | TYR361 |
A | GLY362 |
A | GLN363 |
A | THR364 |
site_id | AC2 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE BCO A 911 |
Chain | Residue |
A | GLN139 |
A | TRP265 |
A | PHE291 |
A | ILE313 |
A | VAL337 |
A | GLY338 |
A | LEU368 |
A | SER469 |
A | GLY470 |
A | TYR471 |
A | ARG501 |
A | LYS532 |
A | PRO537 |
A | TYR538 |
A | TYR540 |
A | ARG542 |
A | AMP901 |
A | HOH919 |
A | HOH937 |
A | HOH943 |
A | HOH1188 |
site_id | AC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE AMP B 902 |
Chain | Residue |
B | GLY338 |
B | GLU339 |
B | SER340 |
B | GLU359 |
B | SER360 |
B | TYR361 |
B | GLY362 |
B | GLN363 |
B | THR364 |
B | ASP446 |
B | PHE458 |
B | ARG461 |
B | ARG472 |
B | BCO912 |
B | HOH1152 |
B | HOH1165 |
site_id | AC4 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE BCO B 912 |
Chain | Residue |
B | GLN139 |
B | LEU267 |
B | PHE291 |
B | ALA311 |
B | ILE313 |
B | VAL337 |
B | GLY338 |
B | LEU368 |
B | SER469 |
B | GLY470 |
B | TYR471 |
B | ARG501 |
B | LYS532 |
B | PRO537 |
B | TYR538 |
B | TYR540 |
B | ARG542 |
B | AMP902 |
B | HOH1109 |
B | HOH1143 |
B | HOH1251 |
B | HOH1349 |
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 | 14 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19345228 |
Chain | Residue | Details |
A | GLN139 | |
B | SER469 | |
B | ARG472 | |
B | ARG501 | |
B | LYS532 | |
B | TYR540 | |
A | THR364 | |
A | SER469 | |
A | ARG472 | |
A | ARG501 | |
A | LYS532 | |
A | TYR540 | |
B | GLN139 | |
B | THR364 |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19345228, ECO:0000269|Ref.7 |
Chain | Residue | Details |
A | THR221 | |
B | LYS557 | |
A | GLU359 | |
A | ASP446 | |
A | ARG461 | |
A | LYS557 | |
B | THR221 | |
B | GLU359 | |
B | ASP446 | |
B | ARG461 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q68CK6 |
Chain | Residue | Details |
A | SER513 | |
B | SER513 |