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5EQT

crystal structure of the ATPase domain of PAN from Pyrococcus horikoshii

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0016887molecular_functionATP hydrolysis activity
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue ADP A 401
ChainResidue
AASP107
ATHR154
ALEU155
AILE285
AHIS289
AGLY312
AALA313
ALYS316
AACT402
AHOH506
AILE108
AGLY109
ALEU111
APRO149
AGLY150
ACYS151
AGLY152
ALYS153

site_idAC2
Number of Residues5
Detailsbinding site for residue ACT A 402
ChainResidue
APRO149
ALYS153
AASN253
AADP401
AHOH506

site_idAC3
Number of Residues1
Detailsbinding site for residue SO4 A 403
ChainResidue
AHIS289

Functional Information from PROSITE/UniProt
site_idPS00674
Number of Residues19
DetailsAAA AAA-protein family signature. VkVIaATNrpdiLDpALl.R
ChainResidueDetails
AVAL246-ARG264

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00553
ChainResidueDetails
AGLY150
AHIS289

219140

PDB entries from 2024-05-01

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