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Cryo-EM structure of the CERU+32/GFP-17 protomer

Analyse Cryo-EM structure of the CERU+32/GFP-17 protomer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6MDR
Type: protein
Length: 3,696 residues
Chains: 16
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CERU+32; GFP-17
UniProt: P42212
Pockets: 20 · best druggability 0.80

Structure

electron microscopy · 2 distinct chains · 8% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
a, c, e, g, i, k, m, o	CERU+32	protein	231	7% helix, 52% strand	P42212
b, d, f, h, j, l, n, p	GFP-17	protein	231	9% helix, 48% strand	P42212

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1063	0.80	0.82	105	empty
2	1118	0.80	0.81	108	empty
3	629	0.79	0.84	66	empty
4	610	0.78	0.84	71	empty
5	638	0.78	0.84	85	empty

Interfaces

28 interfaces between chains.

a–h · 632 Å² buried · 5 hydrogen bonds · protein-protein
i–p · 627 Å² buried · 5 hydrogen bonds · protein-protein
d–e · 626 Å² buried · 5 hydrogen bonds · protein-protein
n–o · 626 Å² buried · 6 hydrogen bonds · protein-protein
j–k · 626 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

6MDR · Cryo-EM structure of the Ceru+32/GFP-17 protomer · the same entry in another collection · chain k against k, 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 P42212
Elsewhere: RCSB PDB 6MDR · PDBe 6MDR · UniProt P42212

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