MolNFT v1 · #169814 · protein + DNA

Structure of RAG1 (R848M/E649V)-RAG2-DNA strand transfer complex (dynamic-form)

6XNX: “Structure of RAG1 (R848M/E649V)-RAG2-DNA strand transfer complex (dynamic-form)”. Electron microscopy, 2 ligands (MG, ZN). MolNFT v1 #169814 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6XNX
Type: protein + DNA
Length: 1,898 residues
Chains: 10
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P15919, P21784
Ligands: MG, ZN

Structure

electron microscopy · 9 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	549	—	P15919
B	—	protein	342	—	P21784
C	—	protein	548	—	P15919
D	—	protein	343	—	P21784
x	—	dna	32	—	—
y	—	dna	28	—	—
I, J	—	dna	14	—	—
L	—	dna	12	—	—
M	—	dna	16	—	—

Ligands and binding sites

MG · Magnesium ion · metal · 4 copies · chains A, y, I, C, x, J
ZN · Zinc ion · metal · 2 copies · chains A, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

6XNX · Structure of RAG1 (R848M/E649V)-RAG2-DNA Strand Transfer Complex (Dynamic-Form) · the same entry in another collection · chain M against M, TM-score 1.00
P15919 · AlphaFold monomer V2.0 prediction for V(D)J recombination-activating protein 1 (P15919) · a predicted model of the same protein · chain A against A, TM-score 0.98

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P15919
Every structure of UniProt P21784
Elsewhere: RCSB PDB 6XNX · PDBe 6XNX · UniProt P15919 · UniProt P21784

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