MolNFT v1 · #19012 · protein

Crystal structure of fkpa from escherichia COLI

1Q6U · Fkbp-type peptidyl-prolyl cis-trans isomerase fkpa: “Crystal structure of fkpa from escherichia COLI”. X-ray diffraction, 1 ligand (CS), 2 pockets (best druggability 0.37). MolNFT v1 #19012 on GenesisL1: 3D structure, binding sites…

PDB: 1Q6U
Type: protein
Length: 213 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fkbp-type peptidyl-prolyl cis-trans isomerase fkpa
EC: 5.2.1.8
UniProt: P45523
Ligands: CS
Pockets: 2 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fkbp-type peptidyl-prolyl cis-trans isomerase fkpa (EC 5.2.1.8)	protein	213	44% helix, 21% strand	P45523

Ligands and binding sites

CS · Cesium ion · metal · chains A

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	136	0.37	0.72	22	empty
2	62	0.36	0.77	12	empty

Compared structures

1Q6U · Crystal structure of FkpA from Escherichia coli · the same entry in another collection · chain A against A, TM-score 1.00
P45523 · AlphaFold monomer V2.0 prediction for fkbp-type peptidyl-prolyl cis- trans isomerase fkpa… · a predicted model of the same protein · chain A against A, TM-score 0.92

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 P45523
Elsewhere: RCSB PDB 1Q6U · PDBe 1Q6U · UniProt P45523

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