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Hsca substrate binding domain complexed with the iscu recognition peptide elppvkihc

Analyse Hsca substrate binding domain complexed with the iscu recognition peptide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1U00
Type: protein
Length: 236 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chaperone protein hsca; Iscu recognition peptide
UniProt: P0A6Z1
Pockets: 2 · best druggability 0.54

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chaperone protein hsca	protein	227	44% helix, 25% strand	P0A6Z1
P	Iscu recognition peptide	protein	9	0% helix, 22% strand	—

Pockets

2 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	191	0.54	0.78	23	empty
2	109	0.39	0.75	20	empty

Interfaces

1 interface between chains.

A–P · 688 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

1U00 · HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC · the same entry in another collection · chain A against A, TM-score 1.00
P0A6Z1 · AlphaFold monomer V2.0 prediction for chaperone protein hsca (P0A6Z1) · 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 P0A6Z1
Elsewhere: RCSB PDB 1U00 · PDBe 1U00 · UniProt P0A6Z1

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