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3W2W

Crystal structure of the Cmr2dHD-Cmr3 subcomplex bound to ATP

Functional Information from GO Data
ChainGOidnamespacecontents
B0000166molecular_functionnucleotide binding
B0003723molecular_functionRNA binding
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0051607biological_processdefense response to virus
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 901
ChainResidue
ACYS448
ACYS451
ACYS478
ACYS481

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ATP A 902
ChainResidue
ASER246
ALEU249
AASN300
AARG436
AASP600
ATYR669
AASP674
AATP903
AHOH1003
AHOH1020
AHOH1038
BARG262
BMG401
ALYS225
AVAL227
AVAL229
AGLN230
AILE233

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ATP A 903
ChainResidue
ATYR271
ALYS301
AASP600
AGLY601
AASP602
AASP603
AMET604
AGLY605
AILE608
AHIS642
ASER646
ALEU649
ALYS739
ALYS744
AATP902
AMG904
AHOH1044
BLYS111

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 904
ChainResidue
AASP600
AGLY601
AATP903
AHOH1044

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG B 401
ChainResidue
AATP902

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:22405013, ECO:0000269|PubMed:22449983, ECO:0000269|PubMed:23395183, ECO:0000269|PubMed:23583914, ECO:0000269|PubMed:25280103
ChainResidueDetails
ACYS448
ACYS451
ACYS478
ACYS481

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:25280103, ECO:0000305|PubMed:22405013
ChainResidueDetails
AASP600
AASP673
AASP674

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:25280103
ChainResidueDetails
AGLU656
AGLU694
AGLU700

226707

PDB entries from 2024-10-30

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