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Structure of O-acetylserine sulfhydrylase in complex with peptide mneni

Analyse Structure of O-acetylserine sulfhydrylase in complex with peptide mneni in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3IQI
Type: protein
Length: 314 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cysteine synthase; Mneni
EC: 2.5.1.47
UniProt: P45040
Pockets: 2 · best druggability 0.52

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	Cysteine synthase (EC 2.5.1.47)	protein	310	43% helix, 18% strand	P45040
P	Mneni	protein	4	0% helix, 0% 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	208	0.52	0.77	36	empty
2	125	0.47	0.78	15	empty

Interfaces

1 interface between chains.

X–P · 411 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (cofactor).

Compared structures

3IQI · Structure of O-Acetylserine Sulfhydrylase in Complex with Peptide MNENI · the same entry in another collection · chain X against X, TM-score 1.00
P45040 · AlphaFold monomer V2.0 prediction for cysteine synthase (P45040) · a predicted model of the same protein · chain X 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 P45040
Elsewhere: RCSB PDB 3IQI · PDBe 3IQI · UniProt P45040

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