MolNFT v1 · #62796 · protein

Crystal structure of fragment 137 to 238 of the human ski-like protein

3EQ5: “Crystal structure of fragment 137 to 238 of the human ski-like protein”. X-ray diffraction, 15 pockets (best druggability 0.66). MolNFT v1 #62796 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3EQ5
Type: protein
Length: 1,156 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ski-like protein
UniProt: P12757
Pockets: 15 · best druggability 0.66

Structure

x-ray diffraction · 9 distinct chains · 40% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ski-like protein	protein	102	42% helix, 24% strand	P12757
B, C	Ski-like protein	protein	97	41% helix, 26% strand	P12757
D	Ski-like protein	protein	96	41% helix, 26% strand	P12757
E	Ski-like protein	protein	95	41% helix, 26% strand	P12757
F	Ski-like protein	protein	98	39% helix, 24% strand	P12757
G	Ski-like protein	protein	95	41% helix, 26% strand	P12757
H	Ski-like protein	protein	96	40% helix, 24% strand	P12757
I, L	Ski-like protein	protein	94	40% helix, 23% strand	P12757
J, K	Ski-like protein	protein	96	39% helix, 25% strand	P12757

Pockets

15 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	503	0.66	0.77	49	empty
2	681	0.65	0.75	64	empty
3	509	0.65	0.77	73	empty
4	494	0.60	0.74	51	empty
5	306	0.58	0.77	42	empty

Interfaces

25 interfaces between chains.

A–B · 665 Å² buried · 15 hydrogen bonds · protein-protein
F–K · 616 Å² buried · 10 hydrogen bonds · protein-protein
E–G · 606 Å² buried · 15 hydrogen bonds · protein-protein
I–J · 605 Å² buried · 11 hydrogen bonds · protein-protein
C–D · 599 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

3EQ5 · Crystal structure of fragment 137 to 238 of the human Ski-like protein · the same entry in another collection · chain L against L, 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 P12757
Elsewhere: RCSB PDB 3EQ5 · PDBe 3EQ5 · UniProt P12757

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