MolNFT v1 · #182500 · protein

Crystal structure of an archaeal cnnm, mtcorb, cbs-pair domain in complex with MG2+-ATP

7MSU · Hemolysin, contains cbs domains: “Crystal structure of an archaeal cnnm, mtcorb, cbs-pair domain in complex with MG2+-ATP”. X-ray diffraction, 2 ligands (ATP, MG), 1 pocket (best druggability 0.36). MolNFT v1 #182500 on GenesisL1…

PDB: 7MSU
Type: protein
Length: 123 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hemolysin, contains cbs domains
UniProt: A0A1G8XA46
Ligands: ATP, MG
Pockets: 1 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hemolysin, contains cbs domains	protein	123	36% helix, 26% strand	A0A1G8XA46

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · chains A
MG · Magnesium ion · metal · 2 copies · chains A
EDO · 1,2-ethanediol · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	69	0.36	0.77	14	ATP

Compared structures

7MSU · Crystal structure of an archaeal CNNM, MtCorB, CBS-pair domain in complex with Mg2+-ATP · 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 A0A1G8XA46
Elsewhere: RCSB PDB 7MSU · PDBe 7MSU · UniProt A0A1G8XA46

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