MolNFT v1 · #122395 · protein

Crystal structure of the C-terminal domain of coenzyme a biosynthesis bifunctional protein coabc

5INT · Phosphopantothenate--cysteine ligase: “Crystal structure of the C-terminal domain of coenzyme a biosynthesis bifunctional protein coabc”. X-ray diffraction, 5 pockets (best druggability 0.49). MolNFT v1 #122395 on GenesisL1: 3D…

PDB: 5INT
Type: protein
Length: 394 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphopantothenate--cysteine ligase
EC: 6.3.2.5
UniProt: Q81WG9
Pockets: 5 · best druggability 0.49

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphopantothenate--cysteine ligase (EC 6.3.2.5)	protein	196	31% helix, 32% strand	Q81WG9
B	Phosphopantothenate--cysteine ligase (EC 6.3.2.5)	protein	198	33% helix, 28% strand	Q81WG9

Pockets

5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	141	0.49	0.79	26	empty
2	135	0.48	0.79	20	empty
3	133	0.44	0.76	33	empty
4	142	0.43	0.76	19	empty
5	81	0.41	0.79	19	empty

Interfaces

1 interface between chains.

A–B · 619 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 modified (engineered).

Compared structures

5INT · Crystal structure of the C-terminal Domain of Coenzyme A biosynthesis bifunctional… · 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 Q81WG9
Elsewhere: RCSB PDB 5INT · PDBe 5INT · UniProt Q81WG9

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