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1YRA

PAB0955 crystal structure : a GTPase in GDP bound form from Pyrococcus abyssi

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GDP A 401
ChainResidue
AGLY10
AALA224
ALYS225
AHOH581
AGLY12
ALYS13
ATHR14
ATHR15
AASN165
ALYS166
AASP168
ASER223

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE GDP B 402
ChainResidue
BGLY10
BSER11
BGLY12
BLYS13
BTHR14
BTHR15
BASN165
BLYS166
BASP168
BLEU169
BSER223
BALA224
BLYS225
BHOH561
BHOH568

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMotif: {"description":"Gly-Pro-Asn (GPN)-loop; involved in dimer interface","evidences":[{"source":"PubMed","id":"17468740","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17468740","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"description":"Stabilizes the phosphate intermediate; shared with dimeric partner","evidences":[{"source":"PubMed","id":"17468740","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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