Research workbench

FK506-binding protein 2

Analyse FK506-binding protein 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2PBC
Type: protein
Length: 398 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: FK506-binding protein 2
EC: 5.2.1.8
UniProt: P26885
Pockets: 7 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 10% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	FK506-binding protein 2 (EC 5.2.1.8)	protein	100	10% helix, 35% strand	P26885
B, D	FK506-binding protein 2 (EC 5.2.1.8)	protein	99	9% helix, 38% strand	P26885

Ligands and binding sites

PEG · Di(hydroxyethyl)ether · additive · 4 copies · chains A, B, C, D

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

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	731	0.73	0.79	59	empty
2	357	0.58	0.75	39	PEG
3	196	0.51	0.77	24	empty
4	72	0.39	0.77	13	PEG
5	62	0.39	0.78	12	PEG

Interfaces

5 interfaces between chains.

A–D · 691 Å² buried · 13 hydrogen bonds · protein-protein
B–C · 507 Å² buried · 9 hydrogen bonds · protein-protein
A–C · 252 Å² buried · 5 hydrogen bonds · protein-protein
B–D · 218 Å² buried · 1 hydrogen bond · protein-protein
C–D · 160 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

2PBC · FK506-binding protein 2 · the same entry in another collection · chain D against D, TM-score 1.00
P26885 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase FKBP2 (P26885) · a predicted model of the same protein · chain D against A, TM-score 0.96

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 P26885
Elsewhere: RCSB PDB 2PBC · PDBe 2PBC · UniProt P26885

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