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5LUL

Structure of a triple variant of cutinase 2 from Thermobifida cellulosilytica

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0042597cellular_componentperiplasmic space
A0050525molecular_functioncutinase activity
A0052689molecular_functioncarboxylic ester hydrolase activity
B0005576cellular_componentextracellular region
B0042597cellular_componentperiplasmic space
B0050525molecular_functioncutinase activity
B0052689molecular_functioncarboxylic ester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CA A 301
ChainResidue
AARG32
AALA35
APHE38
AHOH503
AHOH541
AHOH568

site_idAC2
Number of Residues2
Detailsbinding site for residue CL B 301
ChainResidue
BASN191
BARG257

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 Residues2
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:Q47RJ6
ChainResidueDetails
ASER131
BSER131

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Charge relay system => ECO:0000250|UniProtKB:A0A0K8P6T7
ChainResidueDetails
AASP177
AHIS209
BASP177
BHIS209

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:A0A0K8P6T7
ChainResidueDetails
ATYR61
AMET132
ATRP156
BTYR61
BMET132
BTRP156

219869

PDB entries from 2024-05-15

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