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5LUJ

Structure of cutinase 2 from Thermobifida cellulosilytica

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0016787molecular_functionhydrolase activity
A0042597cellular_componentperiplasmic space
A0050525molecular_functioncutinase activity
A0052689molecular_functioncarboxylic ester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue CL A 301
ChainResidue
AARG29
AARG29

Functional Information from PROSITE/UniProt
site_idPS00120
Number of Residues10
DetailsLIPASE_SER Lipases, serine active site. LAVMGHSMGG
ChainResidueDetails
ALEU125-GLY134

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:Q47RJ6
ChainResidueDetails
ASER131

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000250|UniProtKB:A0A0K8P6T7
ChainResidueDetails
AASP177
AHIS209

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:A0A0K8P6T7
ChainResidueDetails
ATYR61
AMET132
ATRP156

237423

PDB entries from 2025-06-11

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