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3QTG

Crystal structure of pyruvate kinase from Pyrobaculum aerophilum

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004743molecular_functionpyruvate kinase activity
A0006096biological_processglycolytic process
A0030955molecular_functionpotassium ion binding
B0000287molecular_functionmagnesium ion binding
B0004743molecular_functionpyruvate kinase activity
B0006096biological_processglycolytic process
B0030955molecular_functionpotassium ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 500
ChainResidue
ASER381
AMET382
ASER383
AGLY384
ATHR385
ALEU386
ATYR428
AILE450
AHOH491

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 B 500
ChainResidue
AASP108
BSER381
BSER383
BGLY384
BTHR385
BLEU386
BGLY449
BILE450
BHOH467
BHOH517

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 501
ChainResidue
ALEU461
BARG359
BARG451
BGLY452
BHIS455
BHOH518

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

254587

PDB entries from 2026-06-03

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