MolNFT v1 · #154645 · protein

Crystal structure of human asc-card

6KI0 · MALTOSE/MALTODEXTRIN-binding periplasmic PROTEIN,APOPTOSIS…: “Crystal structure of human asc-card”. X-ray diffraction, 2 ligands (GLC, SO4), 8 pockets (best druggability 0.76). MolNFT v1 #154645 on GenesisL1: 3D structure, binding…

PDB: 6KI0
Type: protein
Length: 917 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: MALTOSE/MALTODEXTRIN-binding periplasmic PROTEIN,APOPTOSIS- associated speck-like protein…
UniProt: P0AEX9, Q9ULZ3
Ligands: GLC, SO4
Pockets: 8 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 50% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	MALTOSE/MALTODEXTRIN-binding periplasmic PROTEIN,APOPTOSIS- associated speck-like protein containing a card	protein	459	50% helix, 18% strand	P0AEX9, Q9ULZ3
B	MALTOSE/MALTODEXTRIN-binding periplasmic PROTEIN,APOPTOSIS- associated speck-like protein containing a card	protein	458	49% helix, 17% strand	P0AEX9, Q9ULZ3

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · 6 copies · chains A, B
SO4 · Sulfate ion · ion · 3 copies · chains A, B

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

Pockets

8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	392	0.76	0.85	33	GLC
2	401	0.75	0.85	43	GLC
3	269	0.62	0.81	39	empty
4	269	0.61	0.80	38	empty
5	153	0.42	0.75	30	empty

Interfaces

1 interface between chains.

A–B · 829 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

6KI0 · Crystal Structure of Human ASC-CARD · the same entry in another collection · chain A against A, TM-score 1.00
Q9ULZ3 · AlphaFold monomer V2.0 prediction for apoptosis-associated speck-like protein containing… · a predicted model of the same protein · chain B against A, TM-score 0.19

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 P0AEX9
Every structure of UniProt Q9ULZ3
Elsewhere: RCSB PDB 6KI0 · PDBe 6KI0 · UniProt P0AEX9 · UniProt Q9ULZ3

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