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6V0V

Cryo-EM structure of mouse WT RAG1/2 NFC complex (DNA0)

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
B0002313biological_processmature B cell differentiation involved in immune response
B0002326biological_processB cell lineage commitment
B0002331biological_processpre-B cell allelic exclusion
B0002358biological_processB cell homeostatic proliferation
B0002360biological_processT cell lineage commitment
B0003677molecular_functionDNA binding
B0003682molecular_functionchromatin binding
B0005515molecular_functionprotein binding
B0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
B0005547molecular_functionphosphatidylinositol-3,4,5-trisphosphate binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0006310biological_processDNA recombination
B0006325biological_processchromatin organization
B0008270molecular_functionzinc ion binding
B0030183biological_processB cell differentiation
B0030217biological_processT cell differentiation
B0033077biological_processT cell differentiation in thymus
B0033085biological_processnegative regulation of T cell differentiation in thymus
B0033151biological_processV(D)J recombination
B0035064molecular_functionmethylated histone binding
B0035091molecular_functionphosphatidylinositol binding
B0035265biological_processorgan growth
B0042742biological_processdefense response to bacterium
B0043325molecular_functionphosphatidylinositol-3,4-bisphosphate binding
B0043565molecular_functionsequence-specific DNA binding
B0046622biological_processpositive regulation of organ growth
B0046872molecular_functionmetal ion binding
B0061630molecular_functionubiquitin protein ligase activity
B0080025molecular_functionphosphatidylinositol-3,5-bisphosphate binding
B0097519cellular_componentDNA recombinase complex
B1904155biological_processDN2 thymocyte differentiation
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CA A 1101
ChainResidue
AASP600
AASP708
IDA16
IDC17

site_idAC2
Number of Residues3
Detailsbinding site for residue CA A 1102
ChainResidue
AASP600
AGLU962
IDC17

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 1103
ChainResidue
AHIS937
AHIS942
ACYS727
ACYS730

Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. DTVYILGGHSL
ChainResidueDetails
BASP214-LEU224

site_idPS00518
Number of Residues10
DetailsZF_RING_1 Zinc finger RING-type signature. CkHlFCriCI
ChainResidueDetails
ACYS305-ILE314

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues68
DetailsZN_FING: PHD-type; atypical
ChainResidueDetails
BTRP416-ILE484

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:15964836, ECO:0000269|PubMed:18025461
ChainResidueDetails
BHIS455
BCYS458
BCYS478
BHIS481
BCYS419
BCYS423
BCYS446
BHIS452

site_idSWS_FT_FI3
Number of Residues67
DetailsDNA_BIND: NBD => ECO:0000255|PROSITE-ProRule:PRU00820
ChainResidueDetails
AGLY389-GLN456

site_idSWS_FT_FI4
Number of Residues11
DetailsBINDING: BINDING => ECO:0000269|PubMed:9228952
ChainResidueDetails
ACYS293
AHIS295
ACYS305
AHIS307
ACYS310
ACYS313
ACYS325
ACYS328
ACYS266
AHIS270
ACYS290

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01101, ECO:0000269|PubMed:9228952
ChainResidueDetails
ACYS355
ACYS360
AHIS372
AHIS376

site_idSWS_FT_FI6
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AASP600
AASP708
AGLU962

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Essential for DNA hairpin formation, participates in base-stacking interactions near the cleavage site
ChainResidueDetails
ATRP893

219869

PDB entries from 2024-05-15

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