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

2ECK

STRUCTURE OF PHOSPHOTRANSFERASE

Replaces:  1ECK
Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004017molecular_functionadenylate kinase activity
A0004550molecular_functionnucleoside diphosphate kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006139biological_processnucleobase-containing compound metabolic process
A0006172biological_processADP biosynthetic process
A0009123biological_processnucleoside monophosphate metabolic process
A0009132biological_processnucleoside diphosphate metabolic process
A0009165biological_processnucleotide biosynthetic process
A0015951biological_processpurine ribonucleotide interconversion
A0016208molecular_functionAMP binding
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016776molecular_functionphosphotransferase activity, phosphate group as acceptor
A0019205molecular_functionnucleobase-containing compound kinase activity
A0044209biological_processAMP salvage
A0046940biological_processnucleoside monophosphate phosphorylation
A0050145molecular_functionnucleoside monophosphate kinase activity
B0000287molecular_functionmagnesium ion binding
B0004017molecular_functionadenylate kinase activity
B0004550molecular_functionnucleoside diphosphate kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006139biological_processnucleobase-containing compound metabolic process
B0006172biological_processADP biosynthetic process
B0009123biological_processnucleoside monophosphate metabolic process
B0009132biological_processnucleoside diphosphate metabolic process
B0009165biological_processnucleotide biosynthetic process
B0015951biological_processpurine ribonucleotide interconversion
B0016208molecular_functionAMP binding
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0016776molecular_functionphosphotransferase activity, phosphate group as acceptor
B0019205molecular_functionnucleobase-containing compound kinase activity
B0044209biological_processAMP salvage
B0046940biological_processnucleoside monophosphate phosphorylation
B0050145molecular_functionnucleoside monophosphate kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE AMP A 215
ChainResidue
ATHR31
AHOH217
ALEU35
AARG36
ALYS57
AVAL59
AGLY85
AARG88
AGLN92
AARG156

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ADP A 216
ChainResidue
AGLY10
AALA11
AGLY12
ALYS13
AGLY14
ATHR15
AGLU62
AARG119
AARG123
AVAL132
ATYR133
AHIS134
APHE137
ALYS200
AVAL202
AHOH221

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE AMP B 215
ChainResidue
BTHR31
BLEU35
BARG36
BMET53
BLYS57
BVAL59
BVAL64
BGLY85
BARG88
BGLN92
BARG156
BASP158
BHOH217
BHOH223

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ADP B 216
ChainResidue
BGLY10
BALA11
BGLY12
BLYS13
BGLY14
BTHR15
BGLU62
BARG119
BARG123
BVAL132
BTYR133
BHIS134
BPHE137
BLYS200
BVAL202
BHOH219

Functional Information from PROSITE/UniProt
site_idPS00113
Number of Residues12
DetailsADENYLATE_KINASE Adenylate kinase signature. FLLDGFPRtipQ
ChainResidueDetails
APHE81-GLN92

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00235, ECO:0000269|PubMed:1548697, ECO:0000269|PubMed:16302237, ECO:0000269|PubMed:19805185, ECO:0000269|PubMed:7937733, ECO:0000269|PubMed:8451239
ChainResidueDetails
AGLY10
BTHR31
BARG36
BLYS57
BGLN92
BARG123
BARG156
BLYS200
ATHR31
AARG36
ALYS57
AGLN92
AARG123
AARG156
ALYS200
BGLY10

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00235, ECO:0000269|PubMed:1548697, ECO:0000269|PubMed:19805185, ECO:0000269|PubMed:8451239
ChainResidueDetails
AGLY85
AARG167
BGLY85
BARG167

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:16302237
ChainResidueDetails
AARG119
BARG119

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00235, ECO:0000269|PubMed:1548697, ECO:0000269|PubMed:16302237, ECO:0000269|PubMed:19805185, ECO:0000269|PubMed:8451239
ChainResidueDetails
AVAL132
BVAL132

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS192
BLYS192

Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1zio
ChainResidueDetails
ALYS13
AARG156
AARG123
AARG167
AASP158
AASP159

site_idCSA2
Number of Residues6
DetailsAnnotated By Reference To The Literature 1zio
ChainResidueDetails
BLYS13
BARG156
BARG123
BARG167
BASP158
BASP159

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1zio
ChainResidueDetails
ALYS13
AARG123
AASP33
AGLU162

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1zio
ChainResidueDetails
BLYS13
BARG123
BASP33
BGLU162

224004

PDB entries from 2024-08-21

PDB statisticsPDBj update infoContact PDBjnumon