Research workbench

N160D deamidation mutant of human gammad-crystallin

Analyse N160D deamidation mutant of human gammad-crystallin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6WCY
Type: protein
Length: 343 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Gamma-crystallin D
UniProt: P07320
Ligands: SO4
Pockets: 2 · best druggability 0.58

Structure

x-ray diffraction · 2 distinct chains · 10% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Gamma-crystallin D	protein	172	10% helix, 47% strand	P07320
B	Gamma-crystallin D	protein	171	9% helix, 50% strand	P07320

Ligands and binding sites

SO4 · Sulfate ion · ion · chains B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	287	0.58	0.78	39	empty
2	57	0.28	0.74	17	empty

Interfaces

1 interface between chains.

A–B · 230 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

6WCY · N160D Deamidation Mutant of Human gammaD-Crystallin · the same entry in another collection · chain A against A, TM-score 1.00
P07320 · AlphaFold monomer V2.0 prediction for gamma-crystallin D (P07320) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P07320
Elsewhere: RCSB PDB 6WCY · PDBe 6WCY · UniProt P07320

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