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1DVR

STRUCTURE OF A MUTANT ADENYLATE KINASE LIGATED WITH AN ATP-ANALOGUE SHOWING DOMAIN CLOSURE OVER ATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004017molecular_functionadenylate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005758cellular_componentmitochondrial intermembrane space
A0005829cellular_componentcytosol
A0006139biological_processnucleobase-containing compound metabolic process
A0006172biological_processADP biosynthetic process
A0006270biological_processDNA replication initiation
A0009117biological_processnucleotide metabolic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016740molecular_functiontransferase activity
A0016776molecular_functionphosphotransferase activity, phosphate group as acceptor
A0019205molecular_functionnucleobase-containing compound kinase activity
A0046033biological_processAMP metabolic process
A0046034biological_processATP metabolic process
A0046940biological_processnucleoside monophosphate phosphorylation
B0000166molecular_functionnucleotide binding
B0004017molecular_functionadenylate kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005758cellular_componentmitochondrial intermembrane space
B0005829cellular_componentcytosol
B0006139biological_processnucleobase-containing compound metabolic process
B0006172biological_processADP biosynthetic process
B0006270biological_processDNA replication initiation
B0009117biological_processnucleotide metabolic process
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0016740molecular_functiontransferase activity
B0016776molecular_functionphosphotransferase activity, phosphate group as acceptor
B0019205molecular_functionnucleobase-containing compound kinase activity
B0046033biological_processAMP metabolic process
B0046034biological_processATP metabolic process
B0046940biological_processnucleoside monophosphate phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE ATF A 230
ChainResidue
APRO13
ASER141
ATYR142
AHIS143
APHE146
AALA202
AGLN204
APRO206
AHOH243
AHOH249
AHOH252
AGLY14
AHOH291
BLYS55
BGLN59
BHOH231
AALA15
AGLY16
ALYS17
AGLY18
ATHR19
AARG128
AARG132

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ATF B 230
ChainResidue
ALYS55
AGLN59
BPRO13
BGLY14
BGLY16
BLYS17
BGLY18
BTHR19
BARG128
BARG132
BSER141
BTYR142
BHIS143
BPHE146
BGLN204
BPRO205
BPRO206
BHOH261
BHOH289

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369, ECO:0000269|PubMed:8594191
ChainResidueDetails
AGLN204
BGLY14
BARG132
BGLN204
AGLY14
AARG132

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369
ChainResidueDetails
AGLN97
AILE165
AARG176
BTHR35
BARG40
BGLY61
BGLY90
BGLN97
BILE165
BARG176
ATHR35
AARG40
AGLY61
AGLY90

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:7635152, ECO:0000269|PubMed:7670369, ECO:0000269|PubMed:8594191
ChainResidueDetails
ASER141
BSER141

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:3004985
ChainResidueDetails
ASER1
BSER1

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건을2024-04-17부터공개중

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