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Crystal structure of the xpla heme domain in complex with imidazole and peg

Analyse Crystal structure of the xpla heme domain in complex with imidazole and peg in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4EP6
Type: protein
Length: 392 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome P450-like protein xpla
EC: 1.-.-.-
UniProt: Q8GPH7
Ligands: HEM
Pockets: 2 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome P450-like protein xpla (EC 1.-.-.-)	protein	392	55% helix, 10% strand	Q8GPH7

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
IMD · Imidazole · additive · chains A
1PE · Pentaethylene glycol · additive · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	987	0.86	0.87	92	HEM, IMD, 1PE
2	236	0.53	0.76	24	empty

Compared structures

4EP6 · Crystal structure of the XplA heme domain in complex with imidazole and PEG · 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 Q8GPH7
Elsewhere: RCSB PDB 4EP6 · PDBe 4EP6 · UniProt Q8GPH7

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