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5JPO

Complex structure of human elongation factor 1B gamma GST-liked domain and delta N-terminal domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0006749biological_processglutathione metabolic process
B0006749biological_processglutathione metabolic process
C0006749biological_processglutathione metabolic process
D0006749biological_processglutathione metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue GOL A 301
ChainResidue
ATRP13
AALA110
ASER111
APHE115
ATHR167
ATRP170
AHOH416
AHOH441
AHOH452

site_idAC2
Number of Residues5
Detailsbinding site for residue GOL A 302
ChainResidue
ATHR148
AARG149
CPRO185
CASN186
CARG189

site_idAC3
Number of Residues3
Detailsbinding site for residue GOL A 303
ChainResidue
ATYR7
ALYS52
AGLU62

site_idAC4
Number of Residues9
Detailsbinding site for residue GOL B 301
ChainResidue
BTRP13
BALA110
BSER111
BPHE115
BTHR167
BTRP170
BHOH403
BHOH423
EHOH107

site_idAC5
Number of Residues6
Detailsbinding site for residue GOL D 301
ChainResidue
BTHR148
BGLU155
DPRO185
DASN186
DARG189
DHOH517

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|Ref.9, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712
ChainResidueDetails
EALA2
BALA2
CALA2
DALA2

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ELYS17
BLYS147
CLYS147
DLYS147

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9D8N0
ChainResidueDetails
ALYS212
BLYS212
CLYS212
DLYS212

221051

PDB entries from 2024-06-12

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