MolNFT v1 · #106697 · protein + DNA

Crystal structure of recq catalytic core from C. sakazakii bound to DNA

4TMU: “Crystal structure of recq catalytic core from C. sakazakii bound to DNA”. X-ray diffraction, 1 ligand (ZN), 5 pockets (best druggability 0.84). MolNFT v1 #106697 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4TMU
Type: protein + DNA
Length: 540 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Recq; DNA (29-mer)
UniProt: A7MQK9
Ligands: ZN
Pockets: 5 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Recq	protein	511	46% helix, 15% strand	A7MQK9
B	DNA (29-mer)	dna	29	—	—

Ligands and binding sites

ZN · Zinc ion · metal · chains A

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

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1164	0.84	0.85	82	empty
2	348	0.78	0.88	54	empty
3	375	0.68	0.81	36	empty
4	86	0.35	0.75	20	empty
5	66	0.33	0.76	13	empty

Interfaces

1 interface between chains.

A–B · 1731 Å² buried · 35 hydrogen bonds · protein-nucleic

Compared structures

4TMU · Crystal structure of RecQ catalytic core from C. sakazakii bound to DNA · the same entry in another collection · chain A against A, TM-score 1.00

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 A7MQK9
Elsewhere: RCSB PDB 4TMU · PDBe 4TMU · UniProt A7MQK9

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