1HB8
Structure of bovine Acyl-CoA binding protein in tetragonal crystal form
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000062 | molecular_function | fatty-acyl-CoA binding |
A | 0005783 | cellular_component | endoplasmic reticulum |
A | 0005794 | cellular_component | Golgi apparatus |
A | 0006631 | biological_process | fatty acid metabolic process |
A | 0008289 | molecular_function | lipid binding |
B | 0000062 | molecular_function | fatty-acyl-CoA binding |
B | 0005783 | cellular_component | endoplasmic reticulum |
B | 0005794 | cellular_component | Golgi apparatus |
B | 0006631 | biological_process | fatty acid metabolic process |
B | 0008289 | molecular_function | lipid binding |
C | 0000062 | molecular_function | fatty-acyl-CoA binding |
C | 0005783 | cellular_component | endoplasmic reticulum |
C | 0005794 | cellular_component | Golgi apparatus |
C | 0006631 | biological_process | fatty acid metabolic process |
C | 0008289 | molecular_function | lipid binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 87 |
Chain | Residue |
A | LYS50 |
A | LYS54 |
B | ARG43 |
B | PHE49 |
B | LYS52 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 B 87 |
Chain | Residue |
B | HOH2078 |
B | HOH2079 |
C | ARG43 |
C | PHE49 |
C | LYS52 |
B | LYS50 |
B | LYS54 |
B | HOH2076 |
B | HOH2077 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 C 87 |
Chain | Residue |
A | ARG43 |
A | PHE49 |
A | LYS52 |
B | HOH2015 |
C | LYS50 |
C | LYS54 |
C | HOH2080 |
C | HOH2081 |
C | HOH2082 |
Functional Information from PROSITE/UniProt
site_id | PS00880 |
Number of Residues | 19 |
Details | ACB_1 Acyl-CoA-binding (ACB) domain signature. PAdEeMlfIYShYKQATvG |
Chain | Residue | Details |
A | PRO19-GLY37 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 255 |
Details | Domain: {"description":"ACB","evidences":[{"source":"PROSITE-ProRule","id":"PRU00573","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"8503960","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2003","submissionDatabase":"PDB data bank","title":"RDC-refined NMR structure of bovine acyl-coenzyme A binding protein, ACBP, in complex with palmitoyl-coenzyme A.","authors":["Lerche M.H.","Kragelund B.B.","Redfield C.","Poulsen F.M."]}},{"source":"PDB","id":"1ACA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NVL","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"3525533","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 9 |
Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P31786","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P31786","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P07108","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 3 |
Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P07108","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 3 |
Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P31786","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |