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6ZL7

CRYSTAL STRUCTURE OF C173S MUTATION IN THE PMGL2 ESTERASE FROM PERMAFROST METAGENOMIC LIBRARY

Functional Information from GO Data
ChainGOidnamespacecontents
A0004806molecular_functiontriglyceride lipase activity
A0016787molecular_functionhydrolase activity
B0004806molecular_functiontriglyceride lipase activity
B0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue MG A 401
ChainResidue
AHIS282
AGLU293
ALEU294
AHOH667
BHIS282
BGLU293
BLEU294

site_idAC2
Number of Residues9
Detailsbinding site for residue PG6 A 402
ChainResidue
AGLY203
ATHR204
AALA206
ATYR208
APHE273
AALA274
AALA277
ASER174
AALA175

site_idAC3
Number of Residues9
Detailsbinding site for residue PG6 B 401
ChainResidue
BSER174
BALA175
BCYS202
BGLY203
BTHR204
BALA206
BPHE273
BALA274
BALA277

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PDB entries from 2024-06-12

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