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Crystal structure of plant lectin with two metal binding sites from cicer arietinum at 2.6 ångström resolution

Analyse Crystal structure of plant lectin with two metal binding sites from cicer… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4LL2
Type: protein
Length: 448 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lectin
UniProt: G1K3R9
Ligands: NA, CA, SO4
Pockets: 2 · best druggability 0.39

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Lectin	protein	224	17% helix, 38% strand	G1K3R9

Ligands and binding sites

NA · Sodium ion · metal · chains A
CA · Calcium ion · metal · chains B
SO4 · Sulfate ion · ion · 2 copies · chains A, B
PEG · Di(hydroxyethyl)ether · additive · chains B

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	62	0.39	0.80	14	empty
2	54	0.36	0.79	13	empty

Interfaces

1 interface between chains.

A–B · 688 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

4LL2 · Crystal structure of plant lectin with two metal binding sites from cicer arietinum at… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt G1K3R9
Elsewhere: RCSB PDB 4LL2 · PDBe 4LL2 · UniProt G1K3R9

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