MolNFT v1 · #23882 · protein

Chey mutant with lys 91 replaced by asp, lys 92 replaced by ala, ile 96 replaced by lys and ala 98 replaced by leu (stabilizing mutations in helix 4)

1UDR · Chey protein: “Chey mutant with lys 91 replaced by asp, lys 92 replaced by ala, ile 96 replaced by lys and ala 98 replaced…”. X-ray diffraction, 3 pockets (best druggability 0.67). MolNFT v1 #23882 on GenesisL1: 3D structure…

PDB: 1UDR
Type: protein
Length: 502 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chey protein
UniProt: P06143
Pockets: 3 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, D	Chey protein	protein	126	44% helix, 17% strand	P06143
B, C	Chey protein	protein	125	45% helix, 18% strand	P06143

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	426	0.67	0.79	55	empty
2	231	0.53	0.76	30	empty
3	185	0.49	0.76	24	empty

Interfaces

4 interfaces between chains.

A–D · 511 Å² buried · 4 hydrogen bonds · protein-protein
A–B · 424 Å² buried · 2 hydrogen bonds · protein-protein
C–D · 422 Å² buried · 2 hydrogen bonds · protein-protein
B–D · 53 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

1UDR · Chey mutant with lys 91 replaced by asp, lys 92 replaced by ala, ile 96 replaced by lys… · 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 P06143
Elsewhere: RCSB PDB 1UDR · PDBe 1UDR · UniProt P06143

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