MolNFT v1 · #122757 · protein

Physcomitrella patens fbpase

5IZ1 · Fructose-1,6-bisphosphatase: “Physcomitrella patens fbpase”. X-ray diffraction, 19 pockets (best druggability 0.85). MolNFT v1 #122757 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5IZ1
Type: protein
Length: 1,284 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fructose-1,6-bisphosphatase
UniProt: A9T230
Pockets: 19 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Fructose-1,6-bisphosphatase	protein	321	35% helix, 24% strand	A9T230

Pockets

19 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	515	0.85	0.92	56	empty
2	207	0.68	0.86	27	empty
3	210	0.67	0.85	28	empty
4	212	0.66	0.84	24	empty
5	81	0.65	0.91	32	empty

Interfaces

6 interfaces between chains.

A–B · 2185 Å² buried · 37 hydrogen bonds · protein-protein
C–D · 2175 Å² buried · 35 hydrogen bonds · protein-protein
B–C · 1045 Å² buried · 2 hydrogen bonds · protein-protein
A–D · 1018 Å² buried · 4 hydrogen bonds · protein-protein
B–D · 54 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

5IZ1 · Physcomitrella patens FBPase · 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 A9T230
Elsewhere: RCSB PDB 5IZ1 · PDBe 5IZ1 · UniProt A9T230

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