5CH8
Crystal structure of MDLA N225Q mutant form Penicillium cyclopium
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005576 | cellular_component | extracellular region |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0016042 | biological_process | lipid catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047372 | molecular_function | monoacylglycerol lipase activity |
| A | 0072330 | biological_process | monocarboxylic acid biosynthetic process |
| A | 0120516 | molecular_function | diacylglycerol lipase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 301 |
| Chain | Residue |
| A | GLU129 |
| A | ASP237 |
| A | ASP239 |
| A | HOH606 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue ZN A 302 |
| Chain | Residue |
| A | ASP8 |
| A | GLU43 |
| A | HOH408 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 303 |
| Chain | Residue |
| A | HOH528 |
| A | PHE12 |
| A | ASN73 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 304 |
| Chain | Residue |
| A | TYR21 |
| A | SER145 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 305 |
| Chain | Residue |
| A | THR197 |
| A | ASN224 |
| A | HOH421 |
| A | HOH552 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 306 |
| Chain | Residue |
| A | SER58 |
| A | ILE60 |
| A | THR61 |
| A | HOH409 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 307 |
| Chain | Residue |
| A | LYS33 |
| A | ASP104 |
| A | HOH585 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | binding site for residue GOL A 308 |
| Chain | Residue |
| A | ASP62 |
| A | THR63 |
| A | GLY82 |
| A | SER83 |
| A | GLY111 |
| A | PHE112 |
| A | SER115 |
| A | LEU146 |
| A | VAL150 |
| A | HOH461 |
| A | HOH468 |
Functional Information from PROSITE/UniProt
| site_id | PS00120 |
| Number of Residues | 10 |
| Details | LIPASE_SER Lipases, serine active site. LVVVGHSLGA |
| Chain | Residue | Details |
| A | LEU139-ALA148 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2016","firstPage":"836","lastPage":"839","volume":"4","journal":"ChemistrySelect","title":"Lipase-driven epoxidation is a two-stage synergistic process.","authors":["Tang Q.","Popowicz G.M.","Wang X.","Liu J.","Pavlidis I.V.","Wang Y."],"citationCrossReferences":[{"database":"DOI","id":"10.1002/slct.201600254"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"UniProtKB","id":"P61870","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2016","firstPage":"836","lastPage":"839","volume":"4","journal":"ChemistrySelect","title":"Lipase-driven epoxidation is a two-stage synergistic process.","authors":["Tang Q.","Popowicz G.M.","Wang X.","Liu J.","Pavlidis I.V.","Wang Y."],"citationCrossReferences":[{"database":"DOI","id":"10.1002/slct.201600254"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2016","firstPage":"836","lastPage":"839","volume":"4","journal":"ChemistrySelect","title":"Lipase-driven epoxidation is a two-stage synergistic process.","authors":["Tang Q.","Popowicz G.M.","Wang X.","Liu J.","Pavlidis I.V.","Wang Y."],"citationCrossReferences":[{"database":"DOI","id":"10.1002/slct.201600254"}]}},{"source":"PDB","id":"5CH8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
