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The structure of the C-terminal yada-like domain of BPSL2063 from burkholderia pseudomallei

Analyse The structure of the C-terminal yada-like domain of BPSL2063 from burkholderia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4USX
Type: protein
Length: 633 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Trimeric autotransporter adhesin
UniProt: Q63TA4
Ligands: MG

Structure

x-ray diffraction · 3 distinct chains · 22% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Trimeric autotransporter adhesin	protein	208	22% helix, 26% strand	Q63TA4
B	Trimeric autotransporter adhesin	protein	211	22% helix, 25% strand	Q63TA4
C	Trimeric autotransporter adhesin	protein	214	21% helix, 26% strand	Q63TA4

Ligands and binding sites

MG · Magnesium ion · metal · 7 copies · chains A, C, B

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

Interfaces

3 interfaces between chains.

A–B · 4451 Å² buried · 76 hydrogen bonds · protein-protein
A–C · 4440 Å² buried · 77 hydrogen bonds · protein-protein
B–C · 4429 Å² buried · 74 hydrogen bonds · protein-protein

Compared structures

4USX · The Structure of the C-terminal YadA-like domain of BPSL2063 from Burkholderia… · 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 Q63TA4
Elsewhere: RCSB PDB 4USX · PDBe 4USX · UniProt Q63TA4

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