5LUL

Structure of a triple variant of cutinase 2 from Thermobifida cellulosilytica

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0016787	molecular_function	hydrolase activity
A	0042597	cellular_component	periplasmic space
A	0050525	molecular_function	cutinase activity
A	0052689	molecular_function	carboxylic ester hydrolase activity
B	0005576	cellular_component	extracellular region
B	0016787	molecular_function	hydrolase activity
B	0042597	cellular_component	periplasmic space
B	0050525	molecular_function	cutinase activity
B	0052689	molecular_function	carboxylic ester hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue CA A 301

Chain	Residue
A	ARG32
A	ALA35
A	PHE38
A	HOH503
A	HOH541
A	HOH568

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site_id	AC2
Number of Residues	2
Details	binding site for residue CL B 301

Chain	Residue
B	ASN191
B	ARG257

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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	2
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"Q47RJ6","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
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	6
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"A0A0K8P6T7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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