MolNFT v1 · #145558 · protein + DNA

Crystal structure of recq catalytic core from C. sakazakii bound to an unfolded G-quadruplex

6CRM: “Crystal structure of recq catalytic core from C. sakazakii bound to an unfolded G-quadruplex”. X-ray diffraction, 1 ligand (ZN), 6 pockets (best druggability 0.81). MolNFT v1 #145558 on GenesisL1: 3D structure, binding sites and…

PDB: 6CRM
Type: protein + DNA
Length: 526 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Recq; DNA (5'-D(P*GP*GP*GP*TP*CP*GP*GP*TP*GP*CP*CP*TP*TP*A)-3')
UniProt: A7MQK9
Ligands: ZN
Pockets: 6 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Recq	protein	512	45% helix, 15% strand	A7MQK9
B	DNA (5'-D(PGPGPGPTPCPGPGPTPGPCPCPTPTPA)-3')	dna	14	—	—

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

6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	508	0.81	0.88	70	empty
2	773	0.72	0.78	56	empty
3	476	0.69	0.80	38	empty
4	177	0.66	0.86	24	empty
5	125	0.39	0.74	16	empty

Interfaces

1 interface between chains.

A–B · 1377 Å² buried · 38 hydrogen bonds · protein-nucleic

Compared structures

6CRM · Crystal Structure of RecQ catalytic core from C. sakazakii bound to an unfolded… · 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 6CRM · PDBe 6CRM · UniProt A7MQK9

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