MolNFT v1 · #135879 · protein

Crystal structure of human heme oxygenase-2

5UC8 · Heme oxygenase 2: “Crystal structure of human heme oxygenase-2”. X-ray diffraction, 8 pockets (best druggability 0.76). MolNFT v1 #135879 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5UC8
Type: protein
Length: 839 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Heme oxygenase 2
EC: 1.14.14.18
UniProt: P30519
Pockets: 8 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 76% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Heme oxygenase 2 (EC 1.14.14.18)	protein	209	76% helix, 0% strand	P30519
B, C, D	Heme oxygenase 2 (EC 1.14.14.18)	protein	210	76% helix, 0% strand	P30519

Pockets

8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	483	0.76	0.84	43	empty
2	422	0.76	0.85	39	empty
3	456	0.75	0.84	42	empty
4	1163	0.75	0.77	97	empty
5	505	0.74	0.82	43	empty

Interfaces

5 interfaces between chains.

A–D · 449 Å² buried · 4 hydrogen bonds · protein-protein
B–C · 249 Å² buried · 3 hydrogen bonds · protein-protein
C–D · 241 Å² buried · 1 hydrogen bond · protein-protein
A–C · 134 Å² buried · 0 hydrogen bonds · protein-protein
A–B · 111 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

5UC8 · Crystal structure of human Heme Oxygenase-2 · the same entry in another collection · chain A against A, TM-score 1.00
P30519 · AlphaFold monomer V2.0 prediction for heme oxygenase 2 (P30519) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 P30519
Elsewhere: RCSB PDB 5UC8 · PDBe 5UC8 · UniProt P30519

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