MolNFT v1 · #2656 · protein

T. maritima adenylosuccinate lyase

1C3C · Protein (adenylosuccinate lyase): “T. maritima adenylosuccinate lyase”. X-ray diffraction, 4 pockets (best druggability 0.62). MolNFT v1 #2656 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1C3C
Type: protein
Length: 848 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (adenylosuccinate lyase)
EC: 4.3.2.2
UniProt: Q9X0I0
Pockets: 4 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 66% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protein (adenylosuccinate lyase) (EC 4.3.2.2)	protein	424	66% helix, 5% strand	Q9X0I0

Pockets

4 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	193	0.62	0.83	27	empty
2	339	0.62	0.78	53	empty
3	185	0.62	0.83	21	empty
4	462	0.59	0.75	51	empty

Interfaces

1 interface between chains.

A–B · 1858 Å² buried · 28 hydrogen bonds · protein-protein

Compared structures

1C3C · T. maritima adenylosuccinate lyase · the same entry in another collection · chain A against A, TM-score 1.00
Q9X0I0 · AlphaFold monomer V2.0 prediction for adenylosuccinate lyase (Q9X0I0) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q9X0I0
Elsewhere: RCSB PDB 1C3C · PDBe 1C3C · UniProt Q9X0I0

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