MolNFT v1 · #88902 · protein

Crystal structure of TEP1R

4D94 · Thioester-containing protein 1: “Crystal structure of TEP1R”. X-ray diffraction, 3 ligands (NAG, NA, CL), 12 pockets (best druggability 0.77). MolNFT v1 #88902 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4D94
Type: protein
Length: 1,274 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thioester-containing protein 1
UniProt: C9XI66
Ligands: NAG, NA, CL
Pockets: 12 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 18% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thioester-containing protein 1	protein	1274	18% helix, 44% strand	C9XI66

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 6 copies · chains A
NA · Sodium ion · metal · 2 copies · chains A
CL · Chloride ion · ion · chains A

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

Pockets

12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	723	0.77	0.82	90	empty
2	646	0.72	0.79	76	empty
3	213	0.70	0.86	30	empty
4	725	0.69	0.76	62	empty
5	115	0.68	0.90	24	empty

Modifications

Observed in the structure: 5 glycan, 3 disulfide (N-glycosylation, disulfide).

Compared structures

4D94 · Crystal Structure of TEP1r · 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 C9XI66
Elsewhere: RCSB PDB 4D94 · PDBe 4D94 · UniProt C9XI66

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