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5EE9

Complex structure of OSYCHF1 with GMP-PNP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0009651biological_processresponse to salt stress
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0016887molecular_functionATP hydrolysis activity
A0043022molecular_functionribosome binding
A0043023molecular_functionribosomal large subunit binding
A0046872molecular_functionmetal ion binding
A1900425biological_processnegative regulation of defense response to bacterium
A1901001biological_processnegative regulation of response to salt stress
B0000166molecular_functionnucleotide binding
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0009651biological_processresponse to salt stress
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0016887molecular_functionATP hydrolysis activity
B0043022molecular_functionribosome binding
B0043023molecular_functionribosomal large subunit binding
B0046872molecular_functionmetal ion binding
B1900425biological_processnegative regulation of defense response to bacterium
B1901001biological_processnegative regulation of response to salt stress
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue GNP A 401
ChainResidue
APRO33
AASN230
ACYS264
AMG402
AHOH504
AHOH510
AASN34
AVAL35
AGLY36
ALYS37
ASER38
ATHR39
AGLY97
APHE129

site_idAC2
Number of Residues2
Detailsbinding site for residue MG A 402
ChainResidue
ASER38
AGNP401

site_idAC3
Number of Residues1
Detailsbinding site for residue K B 401
ChainResidue
BTHR258

site_idAC4
Number of Residues6
Detailsbinding site for residue GOL B 402
ChainResidue
BASN34
BVAL35
BGLY36
BLYS37
BSER38
BTHR39

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:26912459, ECO:0007744|PDB:5EE9
ChainResidueDetails
AASN34
APHE129
AASN230
BASN34
BPHE129
BASN230

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01047
ChainResidueDetails
ASER38
BSER263
APHE56
ATHR58
AASP94
ASER263
BSER38
BPHE56
BTHR58
BASP94

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03167
ChainResidueDetails
AMET231
BMET231

237735

PDB entries from 2025-06-18

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