MolNFT v1 · #121813 · protein

Crystal structure of CD-ct domains of chaetomium thermophilum acetyl- CoA carboxylase

5I6H · Acetyl-CoA carboxylase-like protein: “Crystal structure of CD-ct domains of chaetomium thermophilum acetyl- CoA carboxylase”. X-ray diffraction, 20 pockets (best druggability 0.84). MolNFT v1 #121813 on GenesisL1: 3D structure…

PDB: 5I6H
Type: protein
Length: 2,810 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetyl-CoA carboxylase-like protein
UniProt: G0S3L5
Pockets: 20 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acetyl-CoA carboxylase-like protein	protein	1404	40% helix, 15% strand	G0S3L5
B	Acetyl-CoA carboxylase-like protein	protein	1406	40% helix, 16% strand	G0S3L5

Pockets

20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1038	0.84	0.85	89	empty
2	286	0.81	0.92	46	empty
3	286	0.81	0.92	44	empty
4	262	0.81	0.93	33	empty
5	943	0.76	0.79	88	empty

Interfaces

1 interface between chains.

A–B · 7265 Å² buried · 58 hydrogen bonds · protein-protein

Compared structures

5I6H · Crystal structure of CD-CT domains of Chaetomium thermophilum acetyl-CoA carboxylase · 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 G0S3L5
Elsewhere: RCSB PDB 5I6H · PDBe 5I6H · UniProt G0S3L5

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