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Determination of three crystal structures of canavalin by molecular replacement

Analyse Determination of three crystal structures of canavalin by molecular replacement in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1CAW
Type: protein
Length: 365 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Canavalin
UniProt: P50477
Pockets: 5 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 9% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Canavalin	protein	181	7% helix, 40% strand	P50477
B	Canavalin	protein	184	12% helix, 36% strand	P50477

Pockets

5 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	75	0.75	0.98	23	empty
2	134	0.58	0.84	22	empty
3	161	0.51	0.78	23	empty
4	65	0.35	0.77	16	empty
5	53	0.32	0.77	14	empty

Interfaces

1 interface between chains.

A–B · 1629 Å² buried · 23 hydrogen bonds · protein-protein

Compared structures

1CAW · Determination of three crystal structures of canavalin by molecular replacement · the same entry in another collection · chain A against A, TM-score 1.00
P50477 · AlphaFold monomer V2.0 prediction for canavalin (P50477) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 P50477
Elsewhere: RCSB PDB 1CAW · PDBe 1CAW · UniProt P50477

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