Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2IW3

Elongation Factor 3 in complex with ADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0001933biological_processnegative regulation of protein phosphorylation
A0003723molecular_functionRNA binding
A0003746molecular_functiontranslation elongation factor activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005840cellular_componentribosome
A0006412biological_processtranslation
A0006414biological_processtranslational elongation
A0006415biological_processtranslational termination
A0006469biological_processnegative regulation of protein kinase activity
A0010494cellular_componentcytoplasmic stress granule
A0016787molecular_functionhydrolase activity
A0016887molecular_functionATP hydrolysis activity
A0019843molecular_functionrRNA binding
A0022626cellular_componentcytosolic ribosome
A0042788cellular_componentobsolete polysomal ribosome
B0000166molecular_functionnucleotide binding
B0001933biological_processnegative regulation of protein phosphorylation
B0003723molecular_functionRNA binding
B0003746molecular_functiontranslation elongation factor activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005840cellular_componentribosome
B0006412biological_processtranslation
B0006414biological_processtranslational elongation
B0006415biological_processtranslational termination
B0006469biological_processnegative regulation of protein kinase activity
B0010494cellular_componentcytoplasmic stress granule
B0016787molecular_functionhydrolase activity
B0016887molecular_functionATP hydrolysis activity
B0019843molecular_functionrRNA binding
B0022626cellular_componentcytosolic ribosome
B0042788cellular_componentobsolete polysomal ribosome
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A1974
ChainResidue
ASER544
ATRP547
AASN577
AHOH2412

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A1975
ChainResidue
ALYS447
AGLN449
ALYS616
AARG618

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A1976
ChainResidue
AASN583
AASN586
BARG871
AVAL582

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A1977
ChainResidue
AGLU728
AASN729
AARG802
ALYS804
ATYR809
AHOH2291

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A1978
ChainResidue
AGLY465
ACYS466
AGLY467
ALYS468
ASER469
AHOH2413

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B1978
ChainResidue
BTHR259
BALA301
BASP302

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B1979
ChainResidue
BGLU728
BASN729
BARG802
BTYR809
BGLU859
BHOH2405
BHOH2551
BHOH2552

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B1980
ChainResidue
BSER544
BTRP547
BASN577

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B1981
ChainResidue
BLYS447
BGLN449
BLYS616
BARG618
BHOH2273

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B1982
ChainResidue
AARG871
BVAL582
BASN583
BASN586
BHOH2332

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B1983
ChainResidue
BHIS131
BASN134
BLYS966
BHOH2553
BHOH2554

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B1984
ChainResidue
BGLY465
BCYS466
BGLY467
BLYS468
BSER469
BHOH2284

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B1985
ChainResidue
BSER544
BGLY545

site_idBC5
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ADP A1973
ChainResidue
AILE41
AGLU42
AHIS43
AASP44
ASER82
APRO388
ATHR391
AILE392
AHIS395
AGLU396
AASN702
AGLU921
AASN924
AHIS950
AHOH2016
AHOH2411

site_idBC6
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ADP B1977
ChainResidue
BILE41
BGLU42
BHIS43
BASP44
BSER82
BTHR391
BILE392
BHIS395
BGLU396
BASN702
BGLU921
BASN924
BHIS950
BHOH2250
BHOH2393

Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGWKMKLALARAV
ChainResidueDetails
ALEU543-VAL557
ALEU896-THR910

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00434
ChainResidueDetails
APRO463
APRO701
BPRO463
BPRO701

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:9298649, ECO:0007744|PubMed:22814378
ChainResidueDetails
AASP2
BASP2

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:22522802
ChainResidueDetails
AALA187
AALA196
AILE789
BALA187
BALA196
BILE789

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198
ChainResidueDetails
AASN642
AGLY974
BASN642
BGLY974

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
APRO972
BPRO972

site_idSWS_FT_FI6
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
AASP350
AALA636
BASP350
BALA636

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon