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Crystal structure of a post-tailoring hydroxylase (hmtn) involved in the himastatin biosynthesis

Analyse Crystal structure of a post-tailoring hydroxylase (hmtn) involved in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4E2P
Type: protein
Length: 370 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome P450 107B1 (P450CVIIB1)
EC: 1.13.12.-
UniProt: D9WMQ6
Ligands: HEM, MG
Pockets: 3 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome P450 107B1 (P450CVIIB1) (EC 1.13.12.-)	protein	370	51% helix, 12% strand	D9WMQ6

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
MG · Magnesium ion · metal · 4 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	720	0.78	0.82	63	HEM
2	73	0.47	0.82	16	empty
3	69	0.47	0.83	18	empty

Compared structures

4E2P · Crystal Structure of a Post-tailoring Hydroxylase (HmtN) Involved in the Himastatin… · 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 D9WMQ6
Elsewhere: RCSB PDB 4E2P · PDBe 4E2P · UniProt D9WMQ6

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