MolNFT v1 · #146243 · protein + DNA

Cryo-EM structure of rag in complex with one melted rss and one unmelted rss

6DBR: “Cryo-EM structure of rag in complex with one melted rss and one unmelted rss”. Electron microscopy, 2 ligands (CA, ZN). MolNFT v1 #146243 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6DBR
Type: protein + DNA
Length: 1,930 residues
Chains: 8
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P0AEX9, O13033, Q1RLW7
Ligands: CA, ZN

Structure

electron microscopy · 7 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	550	—	P0AEX9, O13033
B, D	—	protein	351	—	Q1RLW7
C	—	protein	542	—	P0AEX9, O13033
E	—	dna	34	—	—
F	—	dna	34	—	—
G	—	dna	34	—	—
H	—	dna	34	—	—

Ligands and binding sites

CA · Calcium ion · metal · 4 copies · chains A, F, C, G
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

6DBR · Cryo-EM structure of RAG in complex with one melted RSS and one unmelted RSS · the same entry in another collection · chain H against H, TM-score 1.00
O13033 · AlphaFold monomer V2.0 prediction for V(D)J recombination-activating protein 1 (O13033) · a predicted model of the same protein · chain C against A, TM-score 0.99

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 P0AEX9
Every structure of UniProt O13033
Every structure of UniProt Q1RLW7
Elsewhere: RCSB PDB 6DBR · PDBe 6DBR · UniProt P0AEX9 · UniProt O13033 · UniProt Q1RLW7

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