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6QLA

CRYSTAL STRUCTURE OF THE PMGL2 ESTERASE (point mutant 1) 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 CL A 401
ChainResidue
AHIS282
AGLU293
ALEU294
BHIS282
BGLU293
BLEU294
BHOH727

site_idAC2
Number of Residues12
Detailsbinding site for residue PG6 A 402
ChainResidue
AALA175
AGLY203
ATHR204
AALA206
ATYR208
APRO235
APHE273
AALA274
APG6403
AHOH658
APHE109
ASER174

site_idAC3
Number of Residues12
Detailsbinding site for residue PG6 A 403
ChainResidue
ASER174
AALA175
AGLY203
ATHR204
AALA206
APRO207
ATYR208
APHE273
AALA277
AHIS302
APG6402
AHOH658

site_idAC4
Number of Residues6
Detailsbinding site for residue MG A 404
ChainResidue
AGLU293
AHOH529
AHOH532
AHOH705
BHOH613
BHOH743

site_idAC5
Number of Residues9
Detailsbinding site for residue PG6 B 401
ChainResidue
BSER174
BALA175
BGLY203
BTHR204
BALA206
BPHE273
BALA274
BALA277
BHOH702

site_idAC6
Number of Residues4
Detailsbinding site for residue MG B 402
ChainResidue
AHOH558
BGLU293
BHOH531
BHOH580

site_idAC7
Number of Residues6
Detailsbinding site for residue MG B 403
ChainResidue
BASN79
BGLU161
BHOH539
BHOH547
BHOH664
BHOH689

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PDB entries from 2024-06-12

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