Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4QRH

Molecular mechanism and evolution of guanylate kinase regulation by (p)ppGpp

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004385molecular_functionGMP kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006163biological_processpurine nucleotide metabolic process
A0009179biological_processpurine ribonucleoside diphosphate metabolic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0046037biological_processGMP metabolic process
A0046710biological_processGDP metabolic process
B0000166molecular_functionnucleotide binding
B0004385molecular_functionGMP kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006163biological_processpurine nucleotide metabolic process
B0009179biological_processpurine ribonucleoside diphosphate metabolic process
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0046037biological_processGMP metabolic process
B0046710biological_processGDP metabolic process
C0000166molecular_functionnucleotide binding
C0004385molecular_functionGMP kinase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006163biological_processpurine nucleotide metabolic process
C0009179biological_processpurine ribonucleoside diphosphate metabolic process
C0016301molecular_functionkinase activity
C0016740molecular_functiontransferase activity
C0046037biological_processGMP metabolic process
C0046710biological_processGDP metabolic process
D0000166molecular_functionnucleotide binding
D0004385molecular_functionGMP kinase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006163biological_processpurine nucleotide metabolic process
D0009179biological_processpurine ribonucleoside diphosphate metabolic process
D0016301molecular_functionkinase activity
D0016740molecular_functiontransferase activity
D0046037biological_processGMP metabolic process
D0046710biological_processGDP metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
AGLY16
AVAL17
AGLY18
ALYS19
AGLY20

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 301
ChainResidue
BTYR78
B0O2303
BHOH558
BHOH559

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE K B 302
ChainResidue
BTYR36
BSER39
BGLU103
B0O2303
BHOH410
BHOH411
BHOH412

site_idAC4
Number of Residues31
DetailsBINDING SITE FOR RESIDUE 0O2 B 303
ChainResidue
BSER15
BGLY16
BVAL17
BGLY18
BLYS19
BGLY20
BSER39
BARG43
BARG46
BTYR55
BGLU74
BALA76
BTYR78
BTYR83
BGLY84
BTHR85
BGLU103
BILE104
BGLU105
BGLY108
BMG301
BK302
BHOH406
BHOH445
BHOH506
BHOH525
BHOH526
BHOH558
BHOH559
BHOH560
BHOH561

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG C 301
ChainResidue
C0O2304
CHOH542

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K C 302
ChainResidue
CTYR36
CSER39
CGLU103
C0O2304
CHOH422
CHOH423

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 303
ChainResidue
CARG43
CGLN44
CASN81
CHOH432
CHOH509

site_idAC8
Number of Residues26
DetailsBINDING SITE FOR RESIDUE 0O2 C 304
ChainResidue
CSER15
CGLY16
CVAL17
CGLY18
CLYS19
CGLY20
CSER39
CARG43
CARG46
CTYR55
CGLU74
CTYR78
CTYR83
CGLY84
CTHR85
CGLU103
CILE104
CGLU105
CGLY108
CMG301
CK302
CHOH443
CHOH481
CHOH503
CHOH541
CHOH542

site_idAC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG D 301
ChainResidue
D0O2306

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE K D 302
ChainResidue
DTYR36
DSER39
DGLU103
D0O2306
DHOH419
DHOH424
DHOH429

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO D 303
ChainResidue
DHOH440

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO D 304
ChainResidue
DHOH423
DALA109
DLYS110
DARG113
DLEU163

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO D 305
ChainResidue
DGLN44
DASN81
DHOH407
DHOH412

site_idBC5
Number of Residues26
DetailsBINDING SITE FOR RESIDUE 0O2 D 306
ChainResidue
DSER15
DGLY16
DVAL17
DGLY18
DLYS19
DGLY20
DSER39
DARG43
DARG46
DTYR55
DGLU74
DTYR78
DTYR83
DGLY84
DTHR85
DGLU103
DILE104
DGLU105
DGLY108
DMG301
DK302
DHOH434
DHOH497
DHOH502
DHOH506
DHOH519

Functional Information from PROSITE/UniProt
site_idPS00856
Number of Residues18
DetailsGUANYLATE_KINASE_1 Guanylate kinase-like signature. TTRqmRegEvdGvdYfFK
ChainResidueDetails
ATHR41-LYS58

246905

PDB entries from 2025-12-31

PDB statisticsPDBj update infoContact PDBjnumon