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Resting state structure of the ompd-domain of human umps variant (K314ACK) at 1.2 ångströms resolution

Analyse Resting state structure of the ompd-domain of human umps variant (K314ACK) at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6ZWZ
Type: protein
Length: 257 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uridine 5'-monophosphate synthase
EC: 2.4.2.10, 4.1.1.23
UniProt: P11172
Ligands: SO4
Pockets: 1 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uridine 5'-monophosphate synthase (EC 2.4.2.10, 4.1.1.23)	protein	257	44% helix, 17% strand	P11172

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	174	0.48	0.76	27	SO4

Modifications

Observed in the structure: 1 modified (acetylation).

Compared structures

6ZWZ · Resting state structure of the OMPD-domain of human UMPS variant (K314AcK) at 1.2… · 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 P11172
Elsewhere: RCSB PDB 6ZWZ · PDBe 6ZWZ · UniProt P11172

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