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6XNX

Structure of RAG1 (R848M/E649V)-RAG2-DNA Strand Transfer Complex (Dynamic-Form)

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
B0005634cellular_componentnucleus
B0006310biological_processDNA recombination
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
D0005634cellular_componentnucleus
D0006310biological_processDNA recombination
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue MG A 1101
ChainResidue
AGLY601
AMET602
yDG35
yDC36

site_idAC2
Number of Residues3
Detailsbinding site for residue MG A 1102
ChainResidue
AGLU662
AASP708
IDC16

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

site_idAC4
Number of Residues6
Detailsbinding site for residue MG C 1101
ChainResidue
CGLY601
CGLU662
CASP708
JDC16
xDC47
xMG101

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN C 1102
ChainResidue
CCYS727
CCYS730
CHIS937
CHIS942

site_idAC6
Number of Residues4
Detailsbinding site for residue MG x 101
ChainResidue
CGLY601
CMG1101
xDG46
xDC47

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 Residues78
DetailsZN_FING: RING-type => ECO:0000255|PROSITE-ProRule:PRU00175
ChainResidueDetails
ACYS290-ARG329
CCYS290-ARG329

site_idSWS_FT_FI2
Number of Residues58
DetailsZN_FING: RAG1-type => ECO:0000255|PROSITE-ProRule:PRU01101
ChainResidueDetails
ALEU351-LYS380
CLEU351-LYS380

site_idSWS_FT_FI3
Number of Residues134
DetailsDNA_BIND: NBD => ECO:0000255|PROSITE-ProRule:PRU00820
ChainResidueDetails
AGLY389-GLN456
CGLY389-GLN456

site_idSWS_FT_FI4
Number of Residues22
DetailsBINDING: BINDING => ECO:0000269|PubMed:9228952
ChainResidueDetails
ACYS266
ACYS325
ACYS328
CCYS266
CHIS270
CCYS290
CCYS293
CHIS295
CCYS305
CHIS307
CCYS310
AHIS270
CCYS313
CCYS325
CCYS328
ACYS290
ACYS293
AHIS295
ACYS305
AHIS307
ACYS310
ACYS313

site_idSWS_FT_FI5
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01101, ECO:0000269|PubMed:9228952
ChainResidueDetails
ACYS355
ACYS360
AHIS372
AHIS376
CCYS355
CCYS360
CHIS372
CHIS376

site_idSWS_FT_FI6
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AASP600
AASP708
AGLU962
CASP600
CASP708
CGLU962

site_idSWS_FT_FI7
Number of Residues2
DetailsSITE: Essential for DNA hairpin formation, participates in base-stacking interactions near the cleavage site
ChainResidueDetails
ATRP893
CTRP893

237735

PDB entries from 2025-06-18

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