Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3QTG

Crystal structure of pyruvate kinase from Pyrobaculum aerophilum

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0004743molecular_functionpyruvate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006096biological_processglycolytic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016740molecular_functiontransferase activity
A0030955molecular_functionpotassium ion binding
A0032869biological_processcellular response to insulin stimulus
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0004743molecular_functionpyruvate kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006096biological_processglycolytic process
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0016740molecular_functiontransferase activity
B0030955molecular_functionpotassium ion binding
B0032869biological_processcellular response to insulin stimulus
B0046872molecular_functionmetal 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: BINDING => ECO:0000250
ChainResidueDetails
AARG46
BASP80
BGLU232
BGLY255
BASP256
BTHR288
AASN48
AASP80
AGLU232
AGLY255
AASP256
ATHR288
BARG46
BASN48

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P14618
ChainResidueDetails
AARG87
ALYS165
BARG87
BLYS165

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000250
ChainResidueDetails
ALYS230
BLYS230

217705

건을2024-03-27부터공개중

PDB statisticsPDBj update infoContact PDBjnumon