7QJQ

Crystal structure of a cutinase enzyme from Thermobifida fusca NTU22 (702)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016787	molecular_function	hydrolase activity
B	0016787	molecular_function	hydrolase activity
C	0016787	molecular_function	hydrolase activity
D	0016787	molecular_function	hydrolase activity
E	0016787	molecular_function	hydrolase activity
F	0016787	molecular_function	hydrolase activity

Functional Information from PROSITE/UniProt

site_id	PS00120
Number of Residues	10
Details	LIPASE_SER Lipases, serine active site. LAVMGHSMGG

Chain	Residue	Details
A	LEU125-GLY134

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"24728714","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4CG2","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	12
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"UniProtKB","id":"A0A0K8P6T7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"A0A0K8P6T7","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"24728714","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"A0A0K8P6T7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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