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Crystal structure of beta-klotho

Analyse Crystal structure of beta-klotho in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5VAN
Type: protein
Length: 983 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q86Z14
Ligands: NAG, MAN, BGC

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	861	—	Q86Z14
B	—	protein	122	—	—

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A
MAN · alpha-D-mannopyranose · sugar · 2 copies
BGC · beta-D-glucopyranose · sugar · 2 copies · chains A
MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A

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

Compared structures

5VAN · Crystal Structure of Beta-Klotho · the same entry in another collection · chain A against A, TM-score 1.00
Q86Z14 · AlphaFold monomer V2.0 prediction for beta-klotho (Q86Z14) · a predicted model of the same protein · 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 Q86Z14
Elsewhere: RCSB PDB 5VAN · PDBe 5VAN · UniProt Q86Z14

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