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1.9 ångström crystal structure of 3-deoxy-manno-octulosonate cytidylyltransferase (kdsb) from acinetobacter baumannii without his- tag bound to the active site

Analyse 1.9 ångström crystal structure of 3-deoxy-manno-octulosonate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4FCU
Type: protein
Length: 253 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3-deoxy-manno-octulosonate cytidylyltransferase
EC: 2.7.7.38
UniProt: A3M4Z0
Pockets: 2 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3-deoxy-manno-octulosonate cytidylyltransferase (EC 2.7.7.38)	protein	253	32% helix, 22% strand	A3M4Z0

Pockets

2 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	467	0.63	0.77	50	empty
2	58	0.37	0.79	13	empty

Compared structures

4FCU · 1.9 Angstrom Crystal Structure of 3-deoxy-manno-octulosonate Cytidylyltransferase (kdsB)… · the same entry in another collection · chain A against A, TM-score 1.00
A3M4Z0 · AlphaFold monomer V2.0 prediction for 3-deoxy-manno-octulosonate cytidylyltransferase… · a predicted model of the same protein · chain A against A, TM-score 0.95

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 A3M4Z0
Elsewhere: RCSB PDB 4FCU · PDBe 4FCU · UniProt A3M4Z0

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