MolNFT v1 · #114159 · protein

Crystal structure of HPIN1 ww domain (5-15) fused with maltose-binding protein in P41212 form

5B3X · Peptidyl-prolyl cis-trans isomerase nima-interacting 1…: “Crystal structure of HPIN1 ww domain (5-15) fused with maltose-binding protein in P41212 form”. X-ray diffraction, 1 ligand (GLC), 3 pockets (best druggability 0.70). MolNFT…

PDB: 5B3X
Type: protein
Length: 377 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptidyl-prolyl cis-trans isomerase nima-interacting 1, maltose-binding periplasmic…
UniProt: Q13526, P0AEX9
Ligands: GLC
Pockets: 3 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidyl-prolyl cis-trans isomerase nima-interacting 1, maltose-binding periplasmic protein	protein	377	41% helix, 20% strand	Q13526, P0AEX9

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A

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

Pockets

3 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	250	0.70	0.85	30	GLC
2	65	0.32	0.76	20	empty
3	67	0.29	0.73	18	empty

Compared structures

5B3X · Crystal structure of hPin1 WW domain (5-15) fused with maltose-binding protein in P41212… · 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 Q13526
Every structure of UniProt P0AEX9
Elsewhere: RCSB PDB 5B3X · PDBe 5B3X · UniProt Q13526 · UniProt P0AEX9

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