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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

3JBY

Cryo-electron microscopy structure of RAG Paired Complex (C2 symmetry)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004519molecular_functionendonuclease activity
A0033151biological_processV(D)J recombination
A0043565molecular_functionsequence-specific DNA binding
A0046872molecular_functionmetal ion binding
A0061630molecular_functionubiquitin protein ligase activity
B0003677molecular_functionDNA binding
B0003682molecular_functionchromatin binding
B0005515molecular_functionprotein binding
B0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
B0005547molecular_functionphosphatidylinositol-3,4,5-trisphosphate binding
B0005634cellular_componentnucleus
B0006310biological_processDNA recombination
B0006325biological_processchromatin organization
B0008270molecular_functionzinc ion binding
B0030098biological_processlymphocyte differentiation
B0030183biological_processB cell differentiation
B0030217biological_processT cell differentiation
B0033077biological_processT cell differentiation in thymus
B0033151biological_processV(D)J recombination
B0033152biological_processimmunoglobulin V(D)J recombination
B0035064molecular_functionmethylated histone binding
B0035091molecular_functionphosphatidylinositol binding
B0043325molecular_functionphosphatidylinositol-3,4-bisphosphate binding
B0043565molecular_functionsequence-specific DNA binding
B0046872molecular_functionmetal ion binding
B0048534biological_processhematopoietic or lymphoid organ development
B0048538biological_processthymus development
B0065004biological_processprotein-DNA complex assembly
B0080025molecular_functionphosphatidylinositol-3,5-bisphosphate binding
B0097519cellular_componentDNA recombinase complex
B1905347cellular_componentendodeoxyribonuclease complex
B1990238molecular_functiondouble-stranded DNA endonuclease activity
C0004519molecular_functionendonuclease activity
C0033151biological_processV(D)J recombination
C0043565molecular_functionsequence-specific DNA binding
C0046872molecular_functionmetal ion binding
C0061630molecular_functionubiquitin protein ligase activity
D0003677molecular_functionDNA binding
D0003682molecular_functionchromatin binding
D0005515molecular_functionprotein binding
D0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
D0005547molecular_functionphosphatidylinositol-3,4,5-trisphosphate binding
D0005634cellular_componentnucleus
D0006310biological_processDNA recombination
D0006325biological_processchromatin organization
D0008270molecular_functionzinc ion binding
D0030098biological_processlymphocyte differentiation
D0030183biological_processB cell differentiation
D0030217biological_processT cell differentiation
D0033077biological_processT cell differentiation in thymus
D0033151biological_processV(D)J recombination
D0033152biological_processimmunoglobulin V(D)J recombination
D0035064molecular_functionmethylated histone binding
D0035091molecular_functionphosphatidylinositol binding
D0043325molecular_functionphosphatidylinositol-3,4-bisphosphate binding
D0043565molecular_functionsequence-specific DNA binding
D0046872molecular_functionmetal ion binding
D0048534biological_processhematopoietic or lymphoid organ development
D0048538biological_processthymus development
D0065004biological_processprotein-DNA complex assembly
D0080025molecular_functionphosphatidylinositol-3,5-bisphosphate binding
D0097519cellular_componentDNA recombinase complex
D1905347cellular_componentendodeoxyribonuclease complex
D1990238molecular_functiondouble-stranded DNA endonuclease activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1101
ChainResidue
ACYS749
ACYS752
AHIS959
AHIS964
site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 1102
ChainResidue
AASP620
AGLY621
AASN987
GDG15
GDT16
site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 1103
ChainResidue
AASP620
AGLU684
AASP730
GDT16
IDA16
site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 1101
ChainResidue
CCYS749
CCYS752
CHIS959
CHIS964
site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 1102
ChainResidue
CASP620
CGLY621
CGLU984
CASN987
FDG15
FDT16
site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA C 1103
ChainResidue
CASP620
CGLU684
CASP730
FDT16
JDA16
Functional Information from PROSITE/UniProt
site_idPS00518
Number of Residues10
DetailsZF_RING_1 Zinc finger RING-type signature. CrHlFCrlCI
ChainResidueDetails
ACYS311-ILE320
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues138
DetailsZN_FING: PHD-type; atypical
ChainResidueDetails
BTRP416-LEU485
DTRP416-LEU485
site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
BCYS419
DCYS423
DCYS446
DHIS453
DHIS456
DCYS459
DCYS479
DHIS482
BCYS423
BCYS446
BHIS453
BHIS456
BCYS459
BCYS479
BHIS482
DCYS419
site_idSWS_FT_FI3
Number of Residues134
DetailsDNA_BIND: NBD => ECO:0000255|PROSITE-ProRule:PRU00820
ChainResidueDetails
AGLY408-GLN475
CGLY408-GLN475
site_idSWS_FT_FI4
Number of Residues28
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ACYS272
ACYS331
ACYS334
AASP620
AASP730
AGLU984
CCYS272
CHIS276
CCYS296
CCYS299
CHIS301
AHIS276
CCYS311
CHIS313
CCYS316
CCYS319
CCYS331
CCYS334
CASP620
CASP730
CGLU984
ACYS296
ACYS299
AHIS301
ACYS311
AHIS313
ACYS316
ACYS319
site_idSWS_FT_FI5
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01101
ChainResidueDetails
ACYS361
ACYS366
AHIS378
AHIS382
CCYS361
CCYS366
CHIS378
CHIS382
site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Essential for DNA hairpin formation, participates in base-stacking interactions near the cleavage site => ECO:0000250
ChainResidueDetails
ATRP915
CTRP915

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PDB entries from 2024-05-01

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