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6LN3

Crystal structure of adenylate kinase from an extremophilic archaeon Aeropyrum pernix with ATP and AMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004017molecular_functionadenylate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016887molecular_functionATP hydrolysis activity
A0046940biological_processnucleoside monophosphate phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue AMP A 301
ChainResidue
AASN40
ATRP109
AGLY111
AARG145
AATP302
AHOH408
AHOH420
AHOH443
AHOH450
AHOH469
AHOH483
APHE41
AGLY42
AMET45
AARG58
AARG62
AGLN73
ATHR98
AHIS99

site_idAC2
Number of Residues27
Detailsbinding site for residue ATP A 302
ChainResidue
APRO14
AGLY15
AVAL16
AGLY17
ALYS18
ATHR19
ATHR20
AHIS99
AARG138
AASP142
AARG145
AARG147
AASN183
AARG184
AGLU185
AGLY186
AALA188
AAMP301
AMG303
AHOH403
AHOH425
AHOH430
AHOH443
AHOH447
AHOH463
AHOH469
AHOH474

site_idAC3
Number of Residues5
Detailsbinding site for residue MG A 303
ChainResidue
ATHR19
AATP302
AHOH430
AHOH443
AHOH469

site_idAC4
Number of Residues13
Detailsbinding site for residue EPE A 304
ChainResidue
ALYS35
APRO65
AARG68
AGLU71
ASER85
ALYS86
AALA87
ALEU88
AGLY89
AHOH426
AHOH429
AHOH432
AHOH530

site_idAC5
Number of Residues5
Detailsbinding site for residue CL A 305
ChainResidue
AGLY12
AALA100
ALEU101
AHOH428
AHOH516

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLY12

224004

PDB entries from 2024-08-21

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