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Plexin A4 full extracellular region, domains 1 to 7 modeled, data to 8 ångström, spacegroup P4(3)2(1)2

Analyse Plexin A4 full extracellular region, domains 1 to 7 modeled, data to 8… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5L5M
Type: protein
Length: 915 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Plexin-A4
UniProt: Q80UG2
Pockets: 11 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Plexin-A4	protein	915	8% helix, 38% strand	Q80UG2

Pockets

11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	475	0.69	0.79	36	empty
2	84	0.65	0.91	29	empty
3	236	0.60	0.80	31	empty
4	104	0.48	0.80	21	empty
5	74	0.44	0.81	19	empty

Modifications

Observed in the structure: 21 disulfide (disulfide).

Compared structures

5L5M · Plexin A4 full extracellular region, domains 1 to 7 modeled, data to 8 angstrom… · the same entry in another collection · chain A against A, TM-score 1.00
Q80UG2 · AlphaFold monomer V2.0 prediction for plexin-A4 (Q80UG2) · a predicted model of the same protein · chain A against A, TM-score 0.73

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 Q80UG2
Elsewhere: RCSB PDB 5L5M · PDBe 5L5M · UniProt Q80UG2

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