1CUD
CUTINASE, N172K, R196D MUTANT, MONOCLINIC CRYSTAL FORM WITH THREE MOLECULES PER ASYMMETRIC UNIT
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005576 | cellular_component | extracellular region |
A | 0016052 | biological_process | carbohydrate catabolic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0050525 | molecular_function | cutinase activity |
A | 0052689 | molecular_function | carboxylic ester hydrolase activity |
B | 0005576 | cellular_component | extracellular region |
B | 0016052 | biological_process | carbohydrate catabolic process |
B | 0016787 | molecular_function | hydrolase activity |
B | 0050525 | molecular_function | cutinase activity |
B | 0052689 | molecular_function | carboxylic ester hydrolase activity |
C | 0005576 | cellular_component | extracellular region |
C | 0016052 | biological_process | carbohydrate catabolic process |
C | 0016787 | molecular_function | hydrolase activity |
C | 0050525 | molecular_function | cutinase activity |
C | 0052689 | molecular_function | carboxylic ester hydrolase activity |
Functional Information from PDB Data
site_id | CAA |
Number of Residues | 3 |
Details | CATALYTIC TRIAD, CHAIN A |
Chain | Residue |
A | SER120 |
A | ASP175 |
A | HIS188 |
site_id | CAB |
Number of Residues | 3 |
Details | CATALYTIC TRIAD, CHAIN B |
Chain | Residue |
B | SER120 |
B | ASP175 |
B | HIS188 |
site_id | CAC |
Number of Residues | 3 |
Details | CATALYTIC TRIAD, CHAIN C |
Chain | Residue |
C | SER120 |
C | ASP175 |
C | HIS188 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"1560844","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AGY","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | Active site: {"evidences":[{"source":"PubMed","id":"1560844","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AGY","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"1560844","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AGY","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"1560844","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8286366","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8555209","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9041628","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AGY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FFE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1OXM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CUT","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"1560844","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8286366","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9041628","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AGY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1OXM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CUT","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1agy |
Chain | Residue | Details |
A | ASP175 | |
A | GLN121 | |
A | SER42 | |
A | SER120 | |
A | HIS188 |
site_id | CSA2 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1agy |
Chain | Residue | Details |
B | ASP175 | |
B | GLN121 | |
B | SER42 | |
B | SER120 | |
B | HIS188 |
site_id | CSA3 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1agy |
Chain | Residue | Details |
C | ASP175 | |
C | GLN121 | |
C | SER42 | |
C | SER120 | |
C | HIS188 |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 631 |
Chain | Residue | Details |
A | SER42 | electrostatic stabiliser |
A | SER120 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
A | GLN121 | electrostatic stabiliser |
A | ASP175 | electrostatic stabiliser, increase basicity |
A | HIS188 | proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 5 |
Details | M-CSA 631 |
Chain | Residue | Details |
B | SER42 | electrostatic stabiliser |
B | SER120 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
B | GLN121 | electrostatic stabiliser |
B | ASP175 | electrostatic stabiliser, increase basicity |
B | HIS188 | proton acceptor, proton donor |
site_id | MCSA3 |
Number of Residues | 5 |
Details | M-CSA 631 |
Chain | Residue | Details |
C | SER42 | electrostatic stabiliser |
C | SER120 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
C | GLN121 | electrostatic stabiliser |
C | ASP175 | electrostatic stabiliser, increase basicity |
C | HIS188 | proton acceptor, proton donor |