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1KVK

The Structure of Binary complex between a Mammalian Mevalonate Kinase and ATP: Insights into the Reaction Mechanism and Human Inherited Disease

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003729molecular_functionmRNA binding
A0004496molecular_functionmevalonate kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005777cellular_componentperoxisome
A0005829cellular_componentcytosol
A0006695biological_processcholesterol biosynthetic process
A0006720biological_processisoprenoid metabolic process
A0008299biological_processisoprenoid biosynthetic process
A0016125biological_processsterol metabolic process
A0016301molecular_functionkinase activity
A0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
A0017148biological_processnegative regulation of translation
A0019287biological_processisopentenyl diphosphate biosynthetic process, mevalonate pathway
A0042802molecular_functionidentical protein binding
A0045540biological_processregulation of cholesterol biosynthetic process
A0046872molecular_functionmetal ion binding
A0050728biological_processnegative regulation of inflammatory response
A1990825molecular_functionsequence-specific mRNA binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 536
ChainResidue
AGLY144
ASER146
AALA147
AGLU193
AHIS197
AASP204
AATP535

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ATP A 535
ChainResidue
AASN104
AGLU105
ASER108
ASER135
AGLY140
AGLY142
AGLY144
ASER145
ASER146
AILE196
AHIS197
AASP204
AMG536
AHOH1020
AHOH1035
AHOH1064
ALYS13
AASN55

Functional Information from PROSITE/UniProt
site_idPS00627
Number of Residues12
DetailsGHMP_KINASES_ATP GHMP kinases putative ATP-binding domain. LPpGaGLGSSAA
ChainResidueDetails
ALEU137-ALA148

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q03426
ChainResidueDetails
ASER146

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q03426
ChainResidueDetails
AASP204

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:11877411, ECO:0007744|PDB:1KVK
ChainResidueDetails
ALYS13
AASN55
AASN104
ASER108
ASER135
ASER146
AGLU193

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:11877411, ECO:0007744|PDB:1KVK, ECO:0007744|PDB:2R42
ChainResidueDetails
AGLY140

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1fwk
ChainResidueDetails
ATHR243

219140

PDB entries from 2024-05-01

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