5LS7
Complex of wild type E. coli alpha aspartate decarboxylase with its processing factor PanZ
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 |
| D | 0004068 | molecular_function | aspartate 1-decarboxylase activity |
| D | 0006523 | biological_process | alanine biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue GOL B 201 |
| Chain | Residue |
| B | ASP99 |
| D | HOH337 |
| B | THR109 |
| B | ALA119 |
| B | GLN120 |
| B | GLY123 |
| B | TRP124 |
| B | HOH314 |
| B | HOH317 |
| B | HOH364 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue PEG B 202 |
| Chain | Residue |
| B | ILE5 |
| B | TYR40 |
| B | GLU84 |
| B | ASN88 |
| B | HOH387 |
| site_id | AC3 |
| Number of Residues | 32 |
| Details | binding site for residue ACO B 203 |
| Chain | Residue |
| B | TYR26 |
| B | SER65 |
| B | LEU66 |
| B | ARG67 |
| B | VAL68 |
| B | ARG73 |
| B | ARG74 |
| B | ARG75 |
| B | GLY76 |
| B | VAL77 |
| B | GLY78 |
| B | GLN79 |
| B | GLY101 |
| B | VAL102 |
| B | GLU103 |
| B | VAL107 |
| B | ALA110 |
| B | PHE111 |
| B | ALA114 |
| B | MG204 |
| B | HOH304 |
| B | HOH318 |
| B | HOH326 |
| B | HOH337 |
| B | HOH370 |
| B | HOH372 |
| B | HOH377 |
| B | HOH404 |
| B | HOH409 |
| B | HOH419 |
| D | ARG102 |
| D | HOH305 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue MG B 204 |
| Chain | Residue |
| B | THR72 |
| B | ARG73 |
| B | ARG74 |
| B | ARG75 |
| B | GLY76 |
| B | VAL77 |
| B | ACO203 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue CO2 B 205 |
| Chain | Residue |
| B | ARG67 |
| B | ARG69 |
| B | GLU70 |
| B | HOH358 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue CO2 B 206 |
| Chain | Residue |
| B | GLU70 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | binding site for residue GOL D 201 |
| Chain | Residue |
| D | GLN30 |
| D | LEU33 |
| D | ASP34 |
| D | GLY37 |
| D | ILE38 |
| D | ARG99 |
| D | HOH302 |
| D | HOH311 |
| D | HOH314 |
| D | HOH320 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue SCN D 202 |
| Chain | Residue |
| D | PVO25 |
| D | ARG54 |
| D | ALA74 |
| D | ALA75 |
| D | ILE86 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue SCN D 203 |
| Chain | Residue |
| A | TYR22 |
| B | ASN45 |
| D | ILE68 |
| D | GLN124 |
| D | VAL125 |
| D | HOH359 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue PEG D 204 |
| Chain | Residue |
| A | HOH121 |
| D | THR92 |
| D | HOH307 |
| D | HOH307 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue 74C D 205 |
| Chain | Residue |
| D | ASP31 |
| D | PHE32 |
| D | MET114 |
| D | HOH399 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue CO2 D 206 |
| Chain | Residue |
| D | GLY110 |
| D | ASP111 |
| D | GLU113 |
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":"Proton donor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
