Research workbench

Crystal structure of ice-binding protein from an antarctic ascomycete, antarctomyces psychrotrophicus.

Analyse Crystal structure of ice-binding protein from an antarctic ascomycete… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7BWY
Type: protein
Length: 609 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ice-binding protein ISOFORM1A
UniProt: A0A2Z6DSM4
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Ice-binding protein ISOFORM1A	protein	203	13% helix, 44% strand	A0A2Z6DSM4

Ligands and binding sites

GOL · Glycerol · additive · 4 copies · chains A, C, B

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

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	353	0.68	0.81	50	empty
2	78	0.51	0.85	25	empty
3	118	0.41	0.76	21	empty

Interfaces

2 interfaces between chains.

A–C · 834 Å² buried · 4 hydrogen bonds · protein-protein
A–B · 686 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

7BWY · Crystal structure of ice-binding protein from an Antarctic ascomycete, Antarctomyces… · 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 A0A2Z6DSM4
Elsewhere: RCSB PDB 7BWY · PDBe 7BWY · UniProt A0A2Z6DSM4

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.