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5IZM

The crystal structure of human eEFSec in complex with GDPNP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0001514biological_processselenocysteine incorporation
A0003746molecular_functiontranslation elongation factor activity
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006412biological_processtranslation
A0016787molecular_functionhydrolase activity
A0035368molecular_functionselenocysteine insertion sequence binding
A0043021molecular_functionribonucleoprotein complex binding
A1990904cellular_componentribonucleoprotein complex
B0000049molecular_functiontRNA binding
B0001514biological_processselenocysteine incorporation
B0003746molecular_functiontranslation elongation factor activity
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0006412biological_processtranslation
B0016787molecular_functionhydrolase activity
B0035368molecular_functionselenocysteine insertion sequence binding
B0043021molecular_functionribonucleoprotein complex binding
B1990904cellular_componentribonucleoprotein complex
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue MN A 1001
ChainResidue
ATHR21
ATHR48
AGNP1002

site_idAC2
Number of Residues18
Detailsbinding site for residue GNP A 1002
ChainResidue
AILE47
ATHR48
AASN146
ALYS147
AASP149
ALEU150
AALA185
AALA186
ALYS187
AGLY189
AGLY190
AMN1001
AILE16
AASP17
AGLY19
ALYS20
ATHR21
AALA22

site_idAC3
Number of Residues3
Detailsbinding site for residue MN B 1001
ChainResidue
BTHR21
BTHR48
BGNP1002

site_idAC4
Number of Residues14
Detailsbinding site for residue GNP B 1002
ChainResidue
BILE16
BSER18
BGLY19
BLYS20
BTHR21
BALA22
BTHR48
BGLY95
BASN146
BLYS147
BASP149
BALA186
BLYS187
BMN1001

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000305|PubMed:27708257
ChainResidueDetails
AGLY19
AALA22
AASP149
ALYS187
BGLY19
BALA22
BASP149
BLYS187

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:27708257, ECO:0007744|PDB:5IZL
ChainResidueDetails
ATHR21
ATHR48
AASP92
BTHR21
BTHR48
BASP92

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER537
BSER537

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9JHW4
ChainResidueDetails
ATHR545
BTHR545

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q9JHW4
ChainResidueDetails
AARG556
BARG556

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PDB entries from 2024-07-24

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