Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4J7N

Crystal structure of mouse DXO in complex with M7GPPPG cap

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0000956biological_processnuclear-transcribed mRNA catabolic process
A0003723molecular_functionRNA binding
A0003729molecular_functionmRNA binding
A0004518molecular_functionnuclease activity
A0004527molecular_functionexonuclease activity
A0005634cellular_componentnucleus
A0005829cellular_componentcytosol
A0006402biological_processmRNA catabolic process
A0008409molecular_function5'-3' exonuclease activity
A0016787molecular_functionhydrolase activity
A0034353molecular_functionmRNA 5'-diphosphatase activity
A0046872molecular_functionmetal ion binding
A0050779biological_processRNA destabilization
A0071028biological_processnuclear mRNA surveillance
A0090304biological_processnucleic acid metabolic process
A0110152molecular_functionRNA NAD+-cap (NAD+-forming) hydrolase activity
A0110155biological_processNAD-cap decapping
Functional Information from PDB Data
site_idAC1
Number of Residues29
DetailsBINDING SITE FOR RESIDUE GTG A 401
ChainResidue
AARG58
ACYS217
AGLY233
AGLU234
ALYS255
ALYS276
ATRP277
AGLN280
A9MG403
AHOH532
AHOH533
AARG95
AHOH587
AHOH646
AHOH652
AHOH682
AHOH699
AHOH702
AHOH708
AHOH868
AHOH877
AHOH899
AGLU97
AGLU101
ATRP131
AARG132
AGLY133
ATHR136
ALYS137

site_idAC2
Number of Residues30
DetailsBINDING SITE FOR RESIDUE GTG A 402
ChainResidue
ATYR70
APRO72
APRO73
APRO74
AILE75
AASN76
AGLN150
AGLU166
APRO168
ALEU303
ALYS304
ATHR305
ASER354
ASER364
AHIS366
ATYR371
AEDO404
AHOH519
AHOH526
AHOH528
AHOH538
AHOH542
AHOH567
AHOH568
AHOH683
AHOH687
AHOH743
AHOH766
AHOH829
AHOH884

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE 9MG A 403
ChainResidue
AGLN280
AGTG401

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 404
ChainResidue
ATYR70
AHIS288
AVAL290
ATHR305
AGTG402
AEDO405
AHOH516
AHOH589
AHOH829

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 405
ChainResidue
AASN239
AVAL365
AEDO404
AHOH829
AHOH928

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:23523372, ECO:0000269|PubMed:28283058
ChainResidueDetails
AARG58
ATRP131
AGLU234
ALYS255
AGLN280

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:23523372
ChainResidueDetails
AGLU101
AGLU192
ACYS217

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:30180947
ChainResidueDetails
AMET185

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:23523372, ECO:0000269|PubMed:30180947
ChainResidueDetails
AASP236

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:23523372, ECO:0000269|PubMed:30180947, ECO:0000305|PubMed:28283058
ChainResidueDetails
AGLU253
ALEU254

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon