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6CIM

Pre-Reaction Complex, RAG1(E962Q)/2-nicked/intact 12/23RSS complex in Mn2+

Functional Information from GO Data
ChainGOidnamespacecontents
A0004519molecular_functionendonuclease activity
A0033151biological_processV(D)J recombination
A0043565molecular_functionsequence-specific DNA 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
C0061630molecular_functionubiquitin protein ligase activity
D0003677molecular_functionDNA binding
D0005634cellular_componentnucleus
D0006310biological_processDNA recombination
N0003677molecular_functionDNA binding
N0005634cellular_componentnucleus
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 1101
ChainResidue
ACYS727
ACYS730
AHIS937
AHIS942

site_idAC2
Number of Residues2
Detailsbinding site for residue MN A 1102
ChainResidue
AASP600
AASP708

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN C 1101
ChainResidue
CHIS942
CCYS727
CCYS730
CHIS937

site_idAC4
Number of Residues3
Detailsbinding site for residue MN C 1102
ChainResidue
CASP600
CGLU662
CASP708

Functional Information from PROSITE/UniProt
site_idPS00353
Number of Residues12
DetailsHMG_BOX_1 HMG box A DNA-binding domain signature. FSKKCsERWKTM
ChainResidueDetails
NPHE41-MET52

site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. DTVYILGGHSL
ChainResidueDetails
BASP214-LEU224

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues70
DetailsDNA_BIND: HMG box 1 => ECO:0000255|PROSITE-ProRule:PRU00267
ChainResidueDetails
NPRO9-ILE79
CGLY389-GLN456

site_idSWS_FT_FI2
Number of Residues68
DetailsDNA_BIND: HMG box 2 => ECO:0000255|PROSITE-ProRule:PRU00267
ChainResidueDetails
NPRO95-ARG163
AASP708
AGLN962
CASP600
CASP708
CGLN962

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P10103
ChainResidueDetails
NMET1
CTRP893

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Cleavage; by thrombin:thrombomodulin => ECO:0000250|UniProtKB:P10103
ChainResidueDetails
NARG10

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Cleavage; by CASP1 => ECO:0000269|PubMed:24474694
ChainResidueDetails
NASP67

site_idSWS_FT_FI6
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P10103
ChainResidueDetails
NLYS3
NLYS7
NLYS8
NLYS12
NLYS28
NLYS29
NLYS127
NLYS128

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Cysteine sulfonic acid (-SO3H); alternate => ECO:0000250|UniProtKB:P63159
ChainResidueDetails
NCYS23
NCYS45

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
NLYS30

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
NSER35

site_idSWS_FT_FI10
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P63158
ChainResidueDetails
NLYS43
NLYS90
NLYS141

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
NSER100

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Cysteine sulfonic acid (-SO3H) => ECO:0000250|UniProtKB:P63159
ChainResidueDetails
NCYS106

site_idSWS_FT_FI13
Number of Residues5
DetailsCROSSLNK: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?) => ECO:0000269|PubMed:29618516
ChainResidueDetails
NLYS28
NLYS43
NLYS44
NLYS68

218853

PDB entries from 2024-04-24

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