MolNFT v1 · #99905 · protein

Crystal structure of human primase catalytic subunit

4MHQ · DNA primase small subunit: “Crystal structure of human primase catalytic subunit”. X-ray diffraction, 1 ligand (ZN), 5 pockets (best druggability 0.47). MolNFT v1 #99905 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4MHQ
Type: protein
Length: 400 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA primase small subunit
EC: 2.7.7.-
UniProt: P49642
Ligands: ZN
Pockets: 5 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA primase small subunit (EC 2.7.7.-)	protein	400	52% helix, 12% strand	P49642

Ligands and binding sites

ZN · Zinc ion · metal · chains A
CIT · Citric acid · additive · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	113	0.47	0.79	17	empty
2	170	0.45	0.75	24	CIT
3	95	0.45	0.79	19	empty
4	79	0.39	0.78	14	empty
5	61	0.32	0.76	12	empty

Compared structures

4MHQ · Crystal structure of human primase catalytic subunit · the same entry in another collection · chain A against A, TM-score 1.00
P49642 · AlphaFold monomer V2.0 prediction for DNA primase small subunit (P49642) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P49642
Elsewhere: RCSB PDB 4MHQ · PDBe 4MHQ · UniProt P49642

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.