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

3KHD

Crystal Structure of PFF1300w.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0004743molecular_functionpyruvate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006096biological_processglycolytic process
A0016301molecular_functionkinase activity
A0030955molecular_functionpotassium ion binding
A0046872molecular_functionmetal ion binding
A0051289biological_processprotein homotetramerization
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0004743molecular_functionpyruvate kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006096biological_processglycolytic process
B0016301molecular_functionkinase activity
B0030955molecular_functionpotassium ion binding
B0046872molecular_functionmetal ion binding
B0051289biological_processprotein homotetramerization
C0000287molecular_functionmagnesium ion binding
C0003824molecular_functioncatalytic activity
C0004743molecular_functionpyruvate kinase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0006096biological_processglycolytic process
C0016301molecular_functionkinase activity
C0030955molecular_functionpotassium ion binding
C0046872molecular_functionmetal ion binding
C0051289biological_processprotein homotetramerization
D0000287molecular_functionmagnesium ion binding
D0003824molecular_functioncatalytic activity
D0004743molecular_functionpyruvate kinase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0006096biological_processglycolytic process
D0016301molecular_functionkinase activity
D0030955molecular_functionpotassium ion binding
D0046872molecular_functionmetal ion binding
D0051289biological_processprotein homotetramerization
Functional Information from PROSITE/UniProt
site_idPS00110
Number of Residues13
DetailsPYRUVATE_KINASE Pyruvate kinase active site signature. IkIIPKIENiEGI
ChainResidueDetails
AILE259-ILE271

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon