4CRY
Direct visualisation of strain-induced protein post-translational modification
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004068 | molecular_function | aspartate 1-decarboxylase activity |
A | 0006523 | biological_process | alanine biosynthetic process |
B | 0005515 | molecular_function | protein binding |
B | 0015940 | biological_process | pantothenate biosynthetic process |
B | 0016485 | biological_process | protein processing |
B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
B | 0031638 | biological_process | zymogen activation |
B | 1905502 | molecular_function | acetyl-CoA binding |
G | 0004068 | molecular_function | aspartate 1-decarboxylase activity |
G | 0006523 | biological_process | alanine biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE ACO B 1128 |
Chain | Residue |
B | TRP23 |
B | ARG75 |
B | GLY76 |
B | VAL77 |
B | GLY78 |
B | GLN79 |
B | GLY101 |
B | VAL102 |
B | GLU103 |
B | MET108 |
B | ALA110 |
B | GLU25 |
B | PHE111 |
B | MG1129 |
B | HOH2032 |
B | HOH2035 |
B | HOH2038 |
B | HOH2055 |
B | HOH2056 |
G | ARG102 |
B | TYR26 |
B | SER65 |
B | LEU66 |
B | ARG67 |
B | VAL68 |
B | ARG73 |
B | ARG74 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG B 1129 |
Chain | Residue |
B | THR72 |
B | ARG73 |
B | ARG74 |
B | ARG75 |
B | GLY76 |
B | VAL77 |
B | ACO1128 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL B 1130 |
Chain | Residue |
A | HOH2004 |
A | HOH2004 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 126 |
Details | Domain: {"description":"N-acetyltransferase","evidences":[{"source":"HAMAP-Rule","id":"MF_02018","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 15 |
Details | Region: {"description":"Interaction with PanD","evidences":[{"source":"PubMed","id":"25910242","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 9 |
Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02018","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25910242","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2008","submissionDatabase":"PDB data bank","title":"Solution NMR structure of putative N-acetyl transferase YhhK from E. coli bound to coenzyme A.","authors":["Cort J.R.","Yee A.","Arrowsmith C.H.","Kennedy M.A."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2014","submissionDatabase":"PDB data bank","title":"Direct visualisation of strain-induced protein post-translational modification.","authors":["Monteiro D.C.F.","Patel V.","Bartlett C.P.","Grant T.D.","Nozaki S.","Gowdy J.A.","Snell E.H.","Niki H.","Pearson A.R.","Webb M.E."]}},{"source":"PDB","id":"2K5T","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Active site: {"description":"Schiff-base intermediate with substrate; via pyruvic acid","evidences":[{"source":"PubMed","id":"9546220","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton donor"} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Pyruvic acid (Ser)","evidences":[{"source":"PubMed","id":"9546220","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
Catalytic Information from CSA