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Crystal Structure Analysis of Maclura pomifera agglutinin

Analyse Crystal Structure Analysis of Maclura pomifera agglutinin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3LLY
Type: protein
Length: 149 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.25
Source: Maclura pomifera
Molecule: Agglutinin alpha chain; Agglutinin beta-2 chain
UniProt: P18674, P18676

Structure

x-ray diffraction · resolution 2.25 · 2 distinct chains · 0% helix, 62% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Agglutinin alpha chain	protein	133	0% helix, 65% strand	P18674
B	Agglutinin beta-2 chain	protein	16	0% helix, 38% strand	P18676

Interfaces

1 interface between chains.

A–B · 529 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

3LLY · Crystal structure analysis of maclura pomifera agglutinin · the same entry in another collection · chain A against A, TM-score 1.00
P18674 · AlphaFold monomer V2.0 prediction for agglutinin alpha chain (P18674) · a predicted model of the same protein · chain A against A, TM-score 0.99
P18676 · AlphaFold monomer V2.0 prediction for agglutinin beta-2 chain (P18676) · a predicted model of the same protein · chain B against A, TM-score 0.25

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 P18674
Every structure of UniProt P18676
Elsewhere: RCSB PDB 3LLY · PDBe 3LLY · UniProt P18674 · UniProt P18676

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