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1S96

The 2.0 A X-ray structure of Guanylate Kinase from E.coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0004385molecular_functionguanylate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006163biological_processpurine nucleotide metabolic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0042802molecular_functionidentical protein binding
A0046037biological_processGMP metabolic process
A0046710biological_processGDP metabolic process
B0004385molecular_functionguanylate kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006163biological_processpurine nucleotide metabolic process
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0042802molecular_functionidentical protein binding
B0046037biological_processGMP metabolic process
B0046710biological_processGDP metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 401
ChainResidue
ASER13
AGLY14
AALA15
AGLY16
AUNX402
AHOH482

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 501
ChainResidue
BHOH633
BGLY14
BALA15
BGLY16

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE UNX A 402
ChainResidue
ASER18
APO4401
AHOH482
AHOH514

Functional Information from PROSITE/UniProt
site_idPS00856
Number of Residues18
DetailsGUANYLATE_KINASE_1 Guanylate kinase-like signature. TTRqpRpgEvhGehYfFV
ChainResidueDetails
ATHR40-VAL57

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AALA11
BALA11

225946

PDB entries from 2024-10-09

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