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4MKH

Crystal structure of a stable adenylate kinase variant AKv18

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
A0008270molecular_functionzinc ion binding
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
A0044209biological_processAMP salvage
A0046872molecular_functionmetal ion binding
A0046940biological_processnucleoside monophosphate phosphorylation
A0050145molecular_functionnucleoside monophosphate kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
ACYS130
ACYS133
ACYS150
AASP153

site_idAC2
Number of Residues37
DetailsBINDING SITE FOR RESIDUE AP5 A 302
ChainResidue
AGLY14
ATHR15
ATHR31
AGLY32
AARG36
AILE53
AGLU57
ALEU58
AVAL59
ATHR64
AGLY85
APHE86
AARG88
AGLN92
AARG123
ALEU124
AARG127
AHIS138
APHE141
AARG160
AARG171
AARG199
AILE201
AHOH404
AHOH407
AHOH421
AHOH423
AHOH424
AHOH455
AHOH459
AHOH486
AHOH488
APRO9
AGLY10
AALA11
AGLY12
ALYS13

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 303
ChainResidue
AMET6
AGLY7
ALEU8
AASN175
AMET179
AEDO304
AHOH497
AHOH498
AHOH499

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 304
ChainResidue
ALEU5
AMET6
AGLY7
ALYS13
AGLY85
APHE86
APRO87
AARG88
AEDO303

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 305
ChainResidue
AASN2
AGLY104
AARG105
AARG128
ALEU157
AHOH508
AHOH509

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues15
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00235, ECO:0000269|PubMed:15100224, ECO:0000269|PubMed:16713575
ChainResidueDetails
AGLY10
ATHR136
ACYS150
AASP153
AARG160
AARG171
AARG199
ATHR31
AARG36
AGLU57
AGLY85
AGLN92
AARG127
ACYS130
ACYS133

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PDB entries from 2024-07-24

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