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5EE3

COMPLEX STRUCTURE OF OSYCHF1 WITH AMP-PNP

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0009651biological_processresponse to salt stress
A0016787molecular_functionhydrolase activity
A0016887molecular_functionATP hydrolysis activity
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
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0009651biological_processresponse to salt stress
B0016787molecular_functionhydrolase activity
B0016887molecular_functionATP hydrolysis activity
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 Residues12
Detailsbinding site for residue ANP A 401
ChainResidue
APRO33
AMET231
ACYS264
AMG402
AASN34
AGLY36
ALYS37
ASER38
ATHR39
AALA96
APHE129
AASN230

site_idAC2
Number of Residues4
Detailsbinding site for residue MG A 402
ChainResidue
ASER38
AASP94
AALA96
AANP401

site_idAC3
Number of Residues2
Detailsbinding site for residue CL A 403
ChainResidue
APHE337
AEPE406

site_idAC4
Number of Residues1
Detailsbinding site for residue CL A 404
ChainResidue
AHIS115

site_idAC5
Number of Residues4
Detailsbinding site for residue EPE A 406
ChainResidue
ATHR309
AGLU314
ATRP318
ACL403

site_idAC6
Number of Residues15
Detailsbinding site for residue ANP B 401
ChainResidue
BLEU32
BASN34
BVAL35
BGLY36
BLYS37
BSER38
BTHR39
BALA96
BPHE129
BASN230
BMET231
BSER263
BCYS264
BALA265
BMG402

site_idAC7
Number of Residues3
Detailsbinding site for residue MG B 402
ChainResidue
BSER38
BASP94
BANP401

site_idAC8
Number of Residues1
Detailsbinding site for residue CL B 404
ChainResidue
BGLU314

site_idAC9
Number of Residues3
Detailsbinding site for residue CL B 405
ChainResidue
BGLY105
BGLU106
BGLY109

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

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PDB entries from 2024-07-24

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