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Trimeric structure of the enzyme iia from escherichia COLI phosphotransferase system specific for N,N'- diacetylchitobiose

Analyse Trimeric structure of the enzyme iia from escherichia COLI phosphotransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1WCR
Type: protein
Length: 309 residues
Chains: 3
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pts system, N, N'-diacetylchitobiose-specific iia component
EC: 2.7.1.69
UniProt: P17335
Pockets: 3 · best druggability 0.54

Structure

solution nmr · 1 distinct chain · 84% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Pts system, N, N'-diacetylchitobiose-specific iia component (EC 2.7.1.69)	protein	103	84% helix, 0% strand	P17335

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	250	0.54	0.76	33	empty
2	208	0.52	0.77	34	empty
3	186	0.51	0.77	29	empty

Interfaces

3 interfaces between chains.

A–B · 950 Å² buried · 4 hydrogen bonds · protein-protein
A–C · 946 Å² buried · 4 hydrogen bonds · protein-protein
B–C · 945 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

1WCR · Trimeric Structure of the Enzyme IIA from Escherichia coli Phosphotransferase System… · 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 P17335
Elsewhere: RCSB PDB 1WCR · PDBe 1WCR · UniProt P17335

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