Research workbench

L-ficolin complexed to N-acetyl-mannosamine

Analyse L-ficolin complexed to N-acetyl-mannosamine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2J0G
Type: protein
Length: 1,289 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q15485

Structure

x-ray diffraction · 6 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	212	—	Q15485
B	—	protein	217	—	Q15485
C	—	protein	216	—	Q15485
D	—	protein	214	—	Q15485
E	—	protein	218	—	Q15485
F	—	protein	212	—	Q15485

Compared structures

2J0G · L-ficolin complexed to N-acetyl-mannosamine · the same entry in another collection · chain F against F, TM-score 1.00
Q15485 · AlphaFold monomer V2.0 prediction for ficolin-2 (Q15485) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q15485
Elsewhere: RCSB PDB 2J0G · PDBe 2J0G · UniProt Q15485

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