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5LUI

Structure of cutinase 1 from Thermobifida cellulosilytica

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0042597cellular_componentperiplasmic space
A0050525molecular_functioncutinase activity
A0052689molecular_functioncarboxylic ester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue PEG A 301
ChainResidue
ATRP156
AILE179
ACL304

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 302
ChainResidue
AASP175
AASP205
AGLU254
AHOH485
AHOH569
AHOH587

site_idAC3
Number of Residues5
Detailsbinding site for residue MG A 303
ChainResidue
AASN29
AHOH402
AHOH404
AHOH425
AHOH657

site_idAC4
Number of Residues4
Detailsbinding site for residue CL A 304
ChainResidue
ATYR61
ASER131
AMET132
APEG301

site_idAC5
Number of Residues3
Detailsbinding site for residue CL A 305
ChainResidue
ACYS260
APRO261
AHOH652

site_idAC6
Number of Residues3
Detailsbinding site for residue CL A 306
ChainResidue
ALEU176
ATHR178
AHIS209

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:A0A0K8P6T7
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

219869

PDB entries from 2024-05-15

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