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Crystal structure of the dib-rm protein

Analyse Crystal structure of the dib-rm protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7L5K
Type: protein
Length: 316 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lipocalin family protein
UniProt: A0A768MZ64
Ligands: SO4
Pockets: 3 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Lipocalin family protein	protein	158	13% helix, 41% strand	A0A768MZ64

Ligands and binding sites

SO4 · Sulfate ion · ion · 12 copies · chains A, B
IPA · Isopropyl alcohol · additive · 4 copies · chains A, B
LMT · Dodecyl-beta-D-maltoside · additive · 4 copies · chains A, 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	341	0.75	0.86	36	LMT
2	435	0.73	0.83	46	LMT
3	59	0.30	0.75	11	empty

Interfaces

1 interface between chains.

A–B · 804 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

7L5K · Crystal structure of the DiB-RM protein · 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 A0A768MZ64
Elsewhere: RCSB PDB 7L5K · PDBe 7L5K · UniProt A0A768MZ64

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