MolNFT v1 · #103494 · protein

Crystal structure of recombinant wt banana lectin

4PIF · Ripening-associated protein: “Crystal structure of recombinant wt banana lectin”. X-ray diffraction, 4 pockets (best druggability 0.67). MolNFT v1 #103494 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4PIF
Type: protein
Length: 562 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ripening-associated protein
UniProt: O22321
Pockets: 4 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 71% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Ripening-associated protein	protein	139	0% helix, 73% strand	O22321
B, D	Ripening-associated protein	protein	142	0% helix, 69% strand	O22321

Ligands and binding sites

GOL · Glycerol · additive · 13 copies · chains A, B, C, D

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	438	0.67	0.79	34	empty
2	103	0.46	0.79	20	empty
3	100	0.41	0.77	17	GOL
4	58	0.40	0.80	14	empty

Interfaces

5 interfaces between chains.

C–D · 782 Å² buried · 15 hydrogen bonds · protein-protein
A–B · 778 Å² buried · 15 hydrogen bonds · protein-protein
A–D · 441 Å² buried · 3 hydrogen bonds · protein-protein
B–C · 439 Å² buried · 4 hydrogen bonds · protein-protein
A–C · 263 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

4PIF · Crystal Structure of recombinant WT Banana Lectin · the same entry in another collection · 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 O22321
Elsewhere: RCSB PDB 4PIF · PDBe 4PIF · UniProt O22321

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