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

4IKE

Crystal Structure of a partly open ATP-lid of liganded Adenylate kinase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004017molecular_functionadenylate kinase activity
A0004550molecular_functionnucleoside diphosphate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006139biological_processnucleobase-containing compound metabolic process
A0009123biological_processnucleoside monophosphate metabolic process
A0009132biological_processnucleoside diphosphate metabolic process
A0009165biological_processnucleotide biosynthetic process
A0016301molecular_functionkinase activity
A0016776molecular_functionphosphotransferase activity, phosphate group as acceptor
A0019205molecular_functionnucleobase-containing compound kinase activity
A0043231cellular_componentintracellular membrane-bounded organelle
A0044209biological_processAMP salvage
A0046940biological_processnucleoside monophosphate phosphorylation
A0050145molecular_functionnucleoside monophosphate kinase activity
B0004017molecular_functionadenylate kinase activity
B0004550molecular_functionnucleoside diphosphate kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006139biological_processnucleobase-containing compound metabolic process
B0009123biological_processnucleoside monophosphate metabolic process
B0009132biological_processnucleoside diphosphate metabolic process
B0009165biological_processnucleotide biosynthetic process
B0016301molecular_functionkinase activity
B0016776molecular_functionphosphotransferase activity, phosphate group as acceptor
B0019205molecular_functionnucleobase-containing compound kinase activity
B0043231cellular_componentintracellular membrane-bounded organelle
B0044209biological_processAMP salvage
B0046940biological_processnucleoside monophosphate phosphorylation
B0050145molecular_functionnucleoside monophosphate kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE AMP A 301
ChainResidue
ATHR31
AGLN89
AARG150
AHOH401
AHOH403
AHOH422
AHOH444
AHOH501
AHOH511
AHOH641
ALEU35
AARG36
AMET53
AGLU57
AVAL59
AILE64
AGLY82
AARG85

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ADP A 302
ChainResidue
AGLY10
AALA11
AGLY12
ALYS13
AGLY14
ATHR15
AARG120
AARG124
ATYR134
AHIS135
ATYR138
ALYS189
APRO190
AVAL191
AHOH418
AHOH436
AHOH501
AHOH517
AHOH520
AHOH633

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE AMP B 301
ChainResidue
BTHR31
BGLY32
BLEU35
BARG36
BMET53
BGLU57
BVAL59
BILE64
BGLY82
BARG85
BGLN89
BHOH415
BHOH418
BHOH421
BHOH425
BHOH433
BHOH437
BHOH476
BHOH477

site_idAC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE ADP B 302
ChainResidue
BGLY10
BALA11
BGLY12
BLYS13
BGLY14
BTHR15
BARG120
BARG124
BLYS189
BPRO190
BVAL191
BHOH422
BHOH437
BHOH461
BHOH463
BHOH500
BHOH517
BHOH523
BHOH579
BHOH611
BHOH635

Functional Information from PROSITE/UniProt
site_idPS00113
Number of Residues12
DetailsADENYLATE_KINASE Adenylate kinase signature. VIFDGFPRtvkQ
ChainResidueDetails
AVAL78-GLN89

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00235, ECO:0000269|PubMed:18026086
ChainResidueDetails
AGLY10
ALYS189
BGLY10
BTHR31
BGLU57
BGLY82
BGLN89
BARG120
BARG124
BVAL133
BARG161
ATHR31
BLYS189
AGLU57
AGLY82
AGLN89
AARG120
AARG124
AVAL133
AARG161

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon