2P8G
Crystal structure of phenolic acid decarboxylase (2635953) from Bacillus subtilis at 1.36 A resolution
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO A 162 |
| Chain | Residue |
| A | HIS8 |
| A | ARG32 |
| A | GLU142 |
| A | VAL143 |
| A | MSE152 |
| A | HOH216 |
| A | HOH380 |
| A | HOH391 |
| A | HOH395 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 163 |
| Chain | Residue |
| A | GLY0 |
| A | ASN3 |
| A | GLY56 |
| A | TYR58 |
| A | PRO76 |
| A | ASN77 |
| A | HOH273 |
| A | HOH402 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 164 |
| Chain | Residue |
| A | PRO76 |
| A | HOH331 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 165 |
| Chain | Residue |
| A | TYR31 |
| A | VAL38 |
| A | GLU64 |
| A | ILE85 |
| A | EDO166 |
| A | HOH188 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 166 |
| Chain | Residue |
| A | TYR11 |
| A | TYR31 |
| A | EDO165 |
| A | HOH185 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 167 |
| Chain | Residue |
| A | LYS79 |
| A | LYS79 |
| A | GLU129 |
| A | GLU129 |
| A | ILE130 |
| A | ILE130 |
| A | HOH411 |
| A | HOH411 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 168 |
| Chain | Residue |
| A | LEU161 |
| A | HOH232 |
| A | HOH364 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 169 |
| Chain | Residue |
| A | LYS52 |
| A | ARG80 |
| A | HOH180 |
| A | HOH335 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| 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 | 1 |
| 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 | 3 |
| 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 |
