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Structure and identification of a pterin dehydratase-like protein as a rubisco assembly factor in the alpha-carboxysome

Analyse Structure and identification of a pterin dehydratase-like protein as a rubisco… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4LOW
Type: protein
Length: 163 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acraf
UniProt: D5X340
Ligands: NI
Pockets: 1 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acraf	protein	84	37% helix, 25% strand	D5X340
B	Acraf	protein	79	41% helix, 27% strand	D5X340

Ligands and binding sites

NI · Nickel (II) ion · metal · 2 copies · chains A
FMT · Formic acid · additive · 6 copies · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	77	0.71	0.95	28	FMT

Interfaces

1 interface between chains.

A–B · 626 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

4LOW · Structure and identification of a pterin dehydratase-like protein as a RuBisCO assembly… · 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 D5X340
Elsewhere: RCSB PDB 4LOW · PDBe 4LOW · UniProt D5X340

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