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

2AR7

Crystal structure of human adenylate kinase 4, AK4

Functional Information from GO Data
ChainGOidnamespacecontents
A0002082biological_processregulation of oxidative phosphorylation
A0004017molecular_functionadenylate kinase activity
A0004550molecular_functionnucleoside diphosphate kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0006139biological_processnucleobase-containing compound metabolic process
A0006172biological_processADP biosynthetic process
A0009117biological_processnucleotide metabolic process
A0009123biological_processnucleoside monophosphate metabolic process
A0009142biological_processnucleoside triphosphate biosynthetic process
A0009188biological_processribonucleoside diphosphate biosynthetic process
A0015949biological_processnucleobase-containing small molecule interconversion
A0016301molecular_functionkinase activity
A0016776molecular_functionphosphotransferase activity, phosphate group as acceptor
A0019205molecular_functionnucleobase-containing compound kinase activity
A0043231cellular_componentintracellular membrane-bounded organelle
A0046033biological_processAMP metabolic process
A0046034biological_processATP metabolic process
A0046039biological_processGTP metabolic process
A0046899molecular_functionnucleoside triphosphate adenylate kinase activity
A0046940biological_processnucleoside monophosphate phosphorylation
A0050145molecular_functionnucleoside monophosphate kinase activity
A0071456biological_processcellular response to hypoxia
B0002082biological_processregulation of oxidative phosphorylation
B0004017molecular_functionadenylate kinase activity
B0004550molecular_functionnucleoside diphosphate kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0006139biological_processnucleobase-containing compound metabolic process
B0006172biological_processADP biosynthetic process
B0009117biological_processnucleotide metabolic process
B0009123biological_processnucleoside monophosphate metabolic process
B0009142biological_processnucleoside triphosphate biosynthetic process
B0009188biological_processribonucleoside diphosphate biosynthetic process
B0015949biological_processnucleobase-containing small molecule interconversion
B0016301molecular_functionkinase activity
B0016776molecular_functionphosphotransferase activity, phosphate group as acceptor
B0019205molecular_functionnucleobase-containing compound kinase activity
B0043231cellular_componentintracellular membrane-bounded organelle
B0046033biological_processAMP metabolic process
B0046034biological_processATP metabolic process
B0046039biological_processGTP metabolic process
B0046899molecular_functionnucleoside triphosphate adenylate kinase activity
B0046940biological_processnucleoside monophosphate phosphorylation
B0050145molecular_functionnucleoside monophosphate kinase activity
B0071456biological_processcellular response to hypoxia
Functional Information from PROSITE/UniProt
site_idPS00113
Number of Residues12
DetailsADENYLATE_KINASE Adenylate kinase signature. WLLDGFPRtlgQ
ChainResidueDetails
ATRP85-GLN96

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03170, ECO:0000269|Ref.17
ChainResidueDetails
AGLY15
BLEU62
BGLY89
BARG126
BARG170
BTHR199
ASER36
ALEU62
AGLY89
AARG126
AARG170
ATHR199
BGLY15
BSER36

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03170
ChainResidueDetails
AARG41
AGLN96
AVAL135
BARG41
BGLN96
BVAL135

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9WUR9
ChainResidueDetails
ALYS60
BLYS60

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9WUR9
ChainResidueDetails
ALYS175
BLYS175

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9WUR9
ChainResidueDetails
ALYS179
ALYS186
BLYS179
BLYS186

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon