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4EB0

Crystal structure of Leaf-branch compost bacterial cutinase homolog

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 Residues5
DetailsBINDING SITE FOR RESIDUE SCN A 301
ChainResidue
AGLY42
ATYR223
AARG286
AHOH452
AHOH527

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SCN A 302
ChainResidue
AHOH469
ATHR96
AARG124
APRO231
AARG290

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SCN A 303
ChainResidue
ASER48
ASER69
ATHR144
ASER145

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SCN A 304
ChainResidue
AARG47
AASN276
AVAL277
AASN278
AASP279
AHOH458
AHOH493
AHOH544

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"24593046","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"32269349","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"24593046","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"32269349","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"A0A0K8P6T7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

244693

PDB entries from 2025-11-12

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