MolNFT v1 · #73996 · protein

Native structure of the udp-N-acetyl-mannosamine dehydrogenase CAP5O from staphylococcus aureus

3OJL: “Native structure of the udp-N-acetyl-mannosamine dehydrogenase CAP5O from staphylococcus aureus”. X-ray diffraction, 1 ligand (NAD), 3 pockets (best druggability 0.76). MolNFT v1 #73996 on GenesisL1: 3D structure, binding sites and…

PDB: 3OJL
Type: protein
Length: 830 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CAP5O
UniProt: P95708
Ligands: NAD
Pockets: 3 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CAP5O	protein	418	40% helix, 14% strand	P95708
B	CAP5O	protein	412	39% helix, 16% strand	P95708

Ligands and binding sites

NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B

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

Pockets

3 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	1002	0.76	0.79	94	NAD
2	1125	0.76	0.78	91	NAD
3	97	0.34	0.74	20	empty

Interfaces

1 interface between chains.

A–B · 2301 Å² buried · 27 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

3OJL · Native structure of the UDP-N-acetyl-mannosamine dehydrogenase Cap5O from Staphylococcus… · the same entry in another collection · chain B against B, 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 P95708
Elsewhere: RCSB PDB 3OJL · PDBe 3OJL · UniProt P95708

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.