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Nucleotide-free form of C. reinhardtii ARSA1

Analyse Nucleotide-free form of C. reinhardtii ARSA1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5ZME
Type: protein
Length: 638 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ATPase ARSA1
EC: 3.6.-.-
UniProt: A8JGB0
Ligands: PO4
Pockets: 9 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ATPase ARSA1 (EC 3.6.-.-)	protein	638	48% helix, 14% strand	A8JGB0

Ligands and binding sites

PO4 · Phosphate ion · ion · 2 copies · chains A

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

Pockets

9 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	973	0.83	0.84	105	PO4
2	732	0.80	0.83	62	empty
3	307	0.64	0.80	36	empty
4	58	0.51	0.86	14	empty
5	115	0.44	0.77	15	empty

Modifications

Observed in the structure: 13 modified (engineered).

Compared structures

5ZME · Nucleotide-free form of C. reinhardtii ArsA1 · the same entry in another collection · chain A against A, TM-score 1.00
A8JGB0 · AlphaFold monomer V2.0 prediction for ATPase ARSA1 (A8JGB0) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 A8JGB0
Elsewhere: RCSB PDB 5ZME · PDBe 5ZME · UniProt A8JGB0

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