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Crystal structure of the signaling protein complex 2

Analyse Crystal structure of the signaling protein complex 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5IXV
Type: protein
Length: 364 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ALR2278 protein
UniProt: Q8YUQ7
Ligands: HEM, 1MZ
Pockets: 2 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	ALR2278 protein	protein	182	54% helix, 17% strand	Q8YUQ7

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
1MZ · 1-methylimidazole · ligand · 2 copies · chains A, B
MLI · Malonate ion · additive · 2 copies · chains A, B

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

Pockets

2 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	620	0.83	0.88	86	HEM, 1MZ, MLI
2	712	0.82	0.86	100	HEM, 1MZ, MLI

Interfaces

1 interface between chains.

A–B · 1129 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

5IXV · Crystal structure of the signaling protein complex 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 Q8YUQ7
Elsewhere: RCSB PDB 5IXV · PDBe 5IXV · UniProt Q8YUQ7

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