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7MHD

Thioesterase Domain of Human Fatty Acid Synthase (FASN-TE) binding a competitive inhibitor SBP-7635

Functional Information from GO Data
ChainGOidnamespacecontents
A0009058biological_processbiosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue ZEP A 601
ChainResidue
AILE250
AALA367
ATYR424
ALEU427
AGLU431
AHIS481
AHOH720
ASER308
ATYR343
AVAL344
ATYR347
ATYR351
AARG352
AALA363
AGLU366

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: For thioesterase activity => ECO:0000255|PROSITE-ProRule:PRU10022, ECO:0000269|PubMed:17618296
ChainResidueDetails
ASER308

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: For thioesterase activity => ECO:0000255|PROSITE-ProRule:PRU10022
ChainResidueDetails
AHIS481

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ATHR215

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ASER236

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P19096
ChainResidueDetails
ALYS391

site_idSWS_FT_FI6
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25114211
ChainResidueDetails
ALYS449

220113

PDB entries from 2024-05-22

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