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6THT

High resolution crystal structure of a Leaf-branch compost cutinase quintuple variant

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0008126molecular_functionacetylesterase activity
A0016787molecular_functionhydrolase activity
A0050525molecular_functioncutinase activity
A0052689molecular_functioncarboxylic ester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue IMD A 301
ChainResidue
ATYR95
ASER148
AALA152
AMET166
ATRP190
AVAL212
AHOH489

site_idAC2
Number of Residues8
Detailsbinding site for residue GOL A 302
ChainResidue
AASP193
ALYS194
ATHR195
AHOH467
AHOH499
AHOH530
AALA59
ATHR60

site_idAC3
Number of Residues11
Detailsbinding site for residue CIT A 303
ChainResidue
AGLY127
APRO128
AASP129
ASER130
AARG151
AHOH422
AHOH423
AHOH435
AHOH520
AHOH560
AHOH694

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:24593046, ECO:0000305|PubMed:32269349
ChainResidueDetails
AALA165

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000305|PubMed:24593046, ECO:0000305|PubMed:32269349
ChainResidueDetails
AASP210
AHIS242

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:A0A0K8P6T7
ChainResidueDetails
ATYR95
AMET166
ATRP190

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PDB entries from 2024-08-21

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