MolNFT v1 · #173778 · protein

Human TENEURIN4 mut C1

7BAO · Teneurin-4: “Human TENEURIN4 mut C1”. Electron microscopy, 2 ligands (NAG, CA), 20 pockets (best druggability 0.86). MolNFT v1 #173778 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7BAO
Type: protein
Length: 1,904 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Teneurin-4
UniProt: Q6N022
Ligands: NAG, CA
Pockets: 20 · best druggability 0.86

Structure

electron microscopy · 1 distinct chain · 7% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Teneurin-4	protein	1904	7% helix, 42% strand	Q6N022

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 15 copies · chains A
CA · Calcium ion · metal · 3 copies · chains A

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

Pockets

20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	639	0.86	0.90	79	empty
2	866	0.83	0.85	91	empty
3	297	0.83	0.94	40	empty
4	694	0.81	0.85	67	empty
5	1173	0.81	0.83	106	empty

Modifications

Observed in the structure: 11 disulfide, 11 glycan (disulfide, N-glycosylation).

Compared structures

7BAO · human Teneurin4 Mut C1 · 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 Q6N022
Elsewhere: RCSB PDB 7BAO · PDBe 7BAO · UniProt Q6N022

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