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Crystal structure of haemophilus influenzae protein HI1011, pfam DUF1537

Analyse Crystal structure of haemophilus influenzae protein HI1011, pfam DUF1537 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1YZY
Type: protein
Length: 824 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein HI1011
UniProt: P44093
Pockets: 9 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Hypothetical protein HI1011	protein	412	42% helix, 20% strand	P44093

Pockets

9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1129	0.72	0.76	102	empty
2	485	0.71	0.81	51	empty
3	203	0.58	0.80	30	empty
4	136	0.51	0.80	22	empty
5	121	0.48	0.79	20	empty

Interfaces

1 interface between chains.

A–B · 673 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

1YZY · Crystal structure of Haemophilus influenzae protein HI1011, Pfam DUF1537 · the same entry in another collection · chain A against A, TM-score 1.00
P44093 · AlphaFold monomer V2.0 prediction for 3-oxo-tetronate kinase (P44093) · a predicted model of the same protein · chain A against A, TM-score 0.88

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 P44093
Elsewhere: RCSB PDB 1YZY · PDBe 1YZY · UniProt P44093

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