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Crystal structure of ATFKBP13

Analyse Crystal structure of ATFKBP13 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1U79
Type: protein
Length: 625 residues
Chains: 5
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fkbp-type peptidyl-prolyl cis-trans isomerase 3
EC: 5.2.1.8
UniProt: Q9SCY2
Pockets: 7 · best druggability 0.41

Structure

x-ray diffraction · 1 distinct chain · 14% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E	Fkbp-type peptidyl-prolyl cis-trans isomerase 3 (EC 5.2.1.8)	protein	125	14% helix, 42% strand	Q9SCY2

Pockets

7 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	104	0.41	0.76	17	empty
2	76	0.36	0.76	15	empty
3	57	0.35	0.77	15	empty
4	57	0.35	0.77	14	empty
5	62	0.34	0.76	12	empty

Interfaces

4 interfaces between chains.

C–E · 683 Å² buried · 6 hydrogen bonds · protein-protein
A–D · 641 Å² buried · 5 hydrogen bonds · protein-protein
A–E · 230 Å² buried · 2 hydrogen bonds · protein-protein
A–B · 23 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide (disulfide).

Compared structures

1U79 · Crystal structure of AtFKBP13 · the same entry in another collection · chain E against E, TM-score 1.00
Q9SCY2 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase FKBP13… · a predicted model of the same protein · chain D against A, TM-score 0.99

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 Q9SCY2
Elsewhere: RCSB PDB 1U79 · PDBe 1U79 · UniProt Q9SCY2

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