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Grifin (crystallisation pH: 4.2)

Analyse Grifin (crystallisation pH: 4.2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5NLZ
Type: protein
Length: 274 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Galectin
UniProt: F1NZ18
Pockets: 1 · best druggability 0.54

Structure

x-ray diffraction · 2 distinct chains · 2% helix, 58% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Galectin	protein	138	2% helix, 57% strand	F1NZ18
B	Galectin	protein	136	2% helix, 60% strand	F1NZ18

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	134	0.54	0.81	25	empty

Interfaces

1 interface between chains.

A–B · 538 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

5NLZ · GRIFIN (Crystallisation pH: 4.2) · 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 F1NZ18
Elsewhere: RCSB PDB 5NLZ · PDBe 5NLZ · UniProt F1NZ18

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