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4CG1

Structural and functional studies on a thermostable polyethylene terephthalate degrading hydrolase from Thermobifida fusca

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 Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 1264
ChainResidue
AVAL24
AARG46
AARG256
ASER257
AHOH2074
AHOH2274
AHOH2334
AHOH2335
AHOH2339

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 1265
ChainResidue
ASER30
AARG31
ALEU32
AARG46
AARG256
AHOH2077
AHOH2340

Functional Information from PROSITE/UniProt
site_idPS00120
Number of Residues10
DetailsLIPASE_SER Lipases, serine active site. LAVMGHSMGG
ChainResidueDetails
ALEU124-GLY133

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:24728714, ECO:0007744|PDB:4CG2
ChainResidueDetails
AILE170

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000250|UniProtKB:A0A0K8P6T7
ChainResidueDetails
ALYS216
ALEU248

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:A0A0K8P6T7, ECO:0000305|PubMed:24728714
ChainResidueDetails
ALEU100
AILE171

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:A0A0K8P6T7
ChainResidueDetails
ASER195

220472

PDB entries from 2024-05-29

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