MolNFT v1 · #120606 · protein

Crystal structure of human GPX4 in complex with gxpep-2

5H5R · Phospholipid hydroperoxide glutathione peroxidase…: “Crystal structure of human GPX4 in complex with gxpep-2”. X-ray diffraction, 2 ligands (ACE, NH2). MolNFT v1 #120606 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5H5R
Type: protein
Length: 182 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phospholipid hydroperoxide glutathione peroxidase, mitochondrial; Gxpep-2
EC: 1.11.1.12
UniProt: P36969
Ligands: ACE, NH2

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phospholipid hydroperoxide glutathione peroxidase, mitochondrial (EC 1.11.1.12)	protein	169	33% helix, 19% strand	P36969
B	Gxpep-2	protein	13	0% helix, 54% strand	—

Ligands and binding sites

ACE · Acetyl group · ligand · chains B
NH2 · Amino group · ion · chains B
GOL · Glycerol · additive · chains A

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

Interfaces

1 interface between chains.

A–B · 606 Å² buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent, 1 disulfide, 1 modified (covalent ligand, disulfide, oxidation).

Compared structures

5H5R · Crystal structure of human GPX4 in complex with GXpep-2 · 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 P36969
Elsewhere: RCSB PDB 5H5R · PDBe 5H5R · UniProt P36969

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