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Structure of P5A-ATPase SPF1, ALF4-bound form

Analyse Structure of P5A-ATPase SPF1, ALF4-bound form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6XMS
Type: protein
Length: 1,091 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: P5A-type ATPase
EC: 7.2.2.-
UniProt: P39986
Ligands: ALF, MG
Pockets: 15 · best druggability 0.82

Structure

electron microscopy · 1 distinct chain · 42% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	P5A-type ATPase (EC 7.2.2.-)	protein	1091	42% helix, 17% strand	P39986

Ligands and binding sites

ALF · Tetrafluoroaluminate ion · ligand · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	912	0.82	0.84	66	empty
2	1008	0.77	0.80	85	MG, ALF
3	519	0.69	0.79	45	empty
4	341	0.66	0.81	48	empty
5	263	0.58	0.78	31	empty

Compared structures

6XMS · Structure of P5A-ATPase Spf1, AlF4-bound form · the same entry in another collection · chain A against A, TM-score 1.00
P39986 · AlphaFold monomer V2.0 prediction for endoplasmic reticulum transmembrane helix… · a predicted model of the same protein · chain A against A, TM-score 0.91

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 P39986
Elsewhere: RCSB PDB 6XMS · PDBe 6XMS · UniProt P39986

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