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Peptide-bound structure of marinomonas primoryensis peptide-binding domain

Analyse Peptide-bound structure of marinomonas primoryensis peptide-binding domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6X6Q
Type: protein
Length: 508 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Antifreeze protein; Asp-ser-asp
UniProt: A1YIY3
Ligands: CA
Pockets: 1 · best druggability 0.44

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Antifreeze protein	protein	505	5% helix, 52% strand	A1YIY3
B	Asp-ser-asp	protein	3	0% helix, 33% strand	—

Ligands and binding sites

CA · Calcium ion · metal · 16 copies · chains A, B
1PE · Pentaethylene glycol · additive · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	189	0.44	0.74	35	empty

Interfaces

1 interface between chains.

A–B · 291 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

6X6Q · Peptide-bound structure of Marinomonas primoryensis peptide-binding domain · 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 A1YIY3
Elsewhere: RCSB PDB 6X6Q · PDBe 6X6Q · UniProt A1YIY3

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