4ALB
Structure of Phenolic Acid Decarboxylase from Bacillus subtilis: Tyr19Ala mutant in complex with coumaric acid
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0009636 | biological_process | response to toxic substance |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0009636 | biological_process | response to toxic substance |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| C | 0009636 | biological_process | response to toxic substance |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016831 | molecular_function | carboxy-lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE HC4 A 1161 |
| Chain | Residue |
| A | TYR11 |
| A | HOH2005 |
| A | TYR13 |
| A | TYR31 |
| A | ILE33 |
| A | ARG41 |
| A | GLU64 |
| A | LEU72 |
| A | ILE85 |
| A | PHE87 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE HC4 B 1161 |
| Chain | Residue |
| B | TYR11 |
| B | TYR13 |
| B | TYR31 |
| B | ARG41 |
| B | GLU64 |
| B | ILE85 |
| B | PHE87 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE HC4 C 1161 |
| Chain | Residue |
| C | TYR11 |
| C | TYR13 |
| C | TYR31 |
| C | ARG41 |
| C | GLU64 |
| C | LEU72 |
| C | ILE85 |
| C | PHE87 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"journal article","publicationDate":"2012","firstPage":"1568","lastPage":"1574","volume":"2","journal":"Catal. Sci. Technol.","title":"Mutational analysis of phenolic acid cecarboxylase from Bacillus subtilis (BsPAD), which converts bio-derived phenolic acids to styrene derivatives.","authors":["Frank A.","Eborall W.","Hyde R.","Hart S.","Turkenburg J.P.","Grogan G."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/C2CY20015E"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2012","firstPage":"1568","lastPage":"1574","volume":"2","journal":"Catal. Sci. Technol.","title":"Mutational analysis of phenolic acid cecarboxylase from Bacillus subtilis (BsPAD), which converts bio-derived phenolic acids to styrene derivatives.","authors":["Frank A.","Eborall W.","Hyde R.","Hart S.","Turkenburg J.P.","Grogan G."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/C2CY20015E"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2012","firstPage":"1568","lastPage":"1574","volume":"2","journal":"Catal. Sci. Technol.","title":"Mutational analysis of phenolic acid cecarboxylase from Bacillus subtilis (BsPAD), which converts bio-derived phenolic acids to styrene derivatives.","authors":["Frank A.","Eborall W.","Hyde R.","Hart S.","Turkenburg J.P.","Grogan G."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/C2CY20015E"}]}}]} |
| Chain | Residue | Details |
