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Crystal structure of TEP1R

Analyse Crystal structure of TEP1R in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2PN5
Type: protein
Length: 1,283 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thioester-containing protein I
UniProt: Q9GYW4
Ligands: NAG, NA
Pockets: 13 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thioester-containing protein I	protein	1283	17% helix, 44% strand	Q9GYW4

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A
NA · Sodium ion · metal · 3 copies · chains A

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

Pockets

13 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	821	0.78	0.82	89	empty
2	691	0.74	0.79	66	empty
3	849	0.73	0.78	61	empty
4	404	0.71	0.82	51	empty
5	125	0.71	0.91	24	empty

Modifications

Observed in the structure: 4 glycan, 3 disulfide (N-glycosylation, disulfide).

Compared structures

2PN5 · 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 Q9GYW4
Elsewhere: RCSB PDB 2PN5 · PDBe 2PN5 · UniProt Q9GYW4

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