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Re-refined structure of a type III antifreeze protein isoform hplc 12

Analyse Re-refined structure of a type III antifreeze protein isoform hplc 12 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7Q3V
Type: protein
Length: 264 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Type-3 ice-structuring protein hplc 12
UniProt: P19614
Pockets: 2 · best druggability 0.41

Structure

x-ray diffraction · 1 distinct chain · 20% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Type-3 ice-structuring protein hplc 12	protein	66	20% helix, 24% strand	P19614

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	61	0.41	0.81	21	empty
2	67	0.28	0.73	14	empty

Interfaces

3 interfaces between chains.

B–C · 371 Å² buried · 7 hydrogen bonds · protein-protein
B–D · 276 Å² buried · 1 hydrogen bond · protein-protein
A–B · 233 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

7Q3V · Re-refined structure of a type III antifreeze protein isoform HPLC 12 · the same entry in another collection · chain D against D, TM-score 1.00
P19614 · AlphaFold monomer V2.0 prediction for type-3 ice-structuring protein hplc 12 (P19614) · a predicted model of the same protein · chain B against A, TM-score 0.97

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 P19614
Elsewhere: RCSB PDB 7Q3V · PDBe 7Q3V · UniProt P19614

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