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2DVO

Structure of PH1917 protein with the complex of ITP from Pyrococcus horikoshii

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005737cellular_componentcytoplasm
A0009117biological_processnucleotide metabolic process
A0009143biological_processnucleoside triphosphate catabolic process
A0009146biological_processpurine nucleoside triphosphate catabolic process
A0016787molecular_functionhydrolase activity
A0017111molecular_functionribonucleoside triphosphate phosphatase activity
A0035870molecular_functiondITP diphosphatase activity
A0036220molecular_functionITP diphosphatase activity
A0036222molecular_functionXTP diphosphatase activity
A0046872molecular_functionmetal ion binding
A0047429molecular_functionnucleoside triphosphate diphosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 301
ChainResidue
ALYS12
ATYR34
AGLU36
AGLU64
AASP65
AITT201

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE ITT A 201
ChainResidue
ALYS12
AGLU36
AGLU64
AASP65
ASER66
AGLY67
ASER81
ASER82
APHE107
APHE140
ATYR142
AASP143
ALYS163
AHIS168
AARG169
ANA301
AHOH318
AHOH325
AHOH341
ATHR7
ASER8
AASN9

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01405
ChainResidueDetails
AASP65

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:18062990, ECO:0000269|Ref.2, ECO:0007744|PDB:2DVO, ECO:0007744|PDB:2E5X
ChainResidueDetails
ATHR7
ASER66
APHE140
ALYS163
AHIS168

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:18062990, ECO:0007744|PDB:2ZTI
ChainResidueDetails
AGLU36
AASP65

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PDB entries from 2024-07-24

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