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1U0L

Crystal structure of YjeQ from Thermotoga maritima

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0016787molecular_functionhydrolase activity
A0019843molecular_functionrRNA binding
A0042254biological_processribosome biogenesis
A0042274biological_processribosomal small subunit biogenesis
A0046872molecular_functionmetal ion binding
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0016787molecular_functionhydrolase activity
B0019843molecular_functionrRNA binding
B0042254biological_processribosome biogenesis
B0042274biological_processribosomal small subunit biogenesis
B0046872molecular_functionmetal ion binding
C0003924molecular_functionGTPase activity
C0005525molecular_functionGTP binding
C0005737cellular_componentcytoplasm
C0016787molecular_functionhydrolase activity
C0019843molecular_functionrRNA binding
C0042254biological_processribosome biogenesis
C0042274biological_processribosomal small subunit biogenesis
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 298
ChainResidue
ACYS250
ACYS255
AHIS257
ACYS263

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 598
ChainResidue
BCYS550
BCYS555
BHIS557
BCYS563

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 898
ChainResidue
CCYS855
CHIS857
CCYS863
CCYS850

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE GDP A 299
ChainResidue
AASN117
ALYS118
AASP120
ALEU121
ASER147
AALA148
ALYS149
AGLY173
AVAL174
AGLY175
ALYS176
ASER177
ASER178
ALEU189

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GDP B 599
ChainResidue
BASN417
BLYS418
BASP420
BLEU421
BSER447
BALA448
BLYS449
BGLY473
BVAL474
BGLY475
BLYS476
BSER477
BSER478

site_idAC6
Number of Residues16
DetailsBINDING SITE FOR RESIDUE GDP C 899
ChainResidue
AVAL269
AGLU270
AASN271
CASN717
CLYS718
CASP720
CLEU721
CSER747
CALA748
CSER772
CGLY773
CVAL774
CGLY775
CLYS776
CSER777
CSER778

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01820, ECO:0000305|PubMed:15331784
ChainResidueDetails
AASN117
AGLY170
BASN417
BGLY470
CASN717
CGLY770

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01820, ECO:0000269|PubMed:15331784
ChainResidueDetails
ACYS250
ACYS255
ACYS263
BCYS550
BCYS555
BCYS563
CCYS850
CCYS855
CCYS863

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15331784
ChainResidueDetails
AHIS257
BHIS557
CHIS857

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PDB entries from 2024-07-31

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