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Crystal structure of malignant T cell-amplified sequence 1 protein

Analyse Crystal structure of malignant T cell-amplified sequence 1 protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3R90
Type: protein
Length: 2,201 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Malignant T cell-amplified sequence 1
UniProt: Q9ULC4
Ligands: UNX, SO4
Pockets: 19 · best druggability 0.87

Structure

x-ray diffraction · 5 distinct chains · 32% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Malignant T cell-amplified sequence 1	protein	185	36% helix, 29% strand	Q9ULC4
D, H, L	Malignant T cell-amplified sequence 1	protein	180	29% helix, 29% strand	Q9ULC4
E, F, G	Malignant T cell-amplified sequence 1	protein	181	35% helix, 33% strand	Q9ULC4
I	Malignant T cell-amplified sequence 1	protein	187	31% helix, 29% strand	Q9ULC4
J, K	Malignant T cell-amplified sequence 1	protein	188	31% helix, 28% strand	Q9ULC4

Ligands and binding sites

UNX · Unknown atom or ion · ion · 174 copies · chains A, H, B, G, C, D, K, E, F, I, L, J
SO4 · Sulfate ion · ion · 25 copies · chains A, B, G, H, L, C, K, D, J, E, I, F
GOL · Glycerol · additive · chains L

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	957	0.87	0.88	126	SO4, UNX
2	876	0.86	0.88	115	SO4, UNX
3	1111	0.85	0.86	125	SO4, UNX
4	1094	0.85	0.85	121	UNX, SO4
5	535	0.84	0.89	64	UNX

Interfaces

26 interfaces between chains.

E–I · 832 Å² buried · 6 hydrogen bonds · protein-protein
B–L · 827 Å² buried · 7 hydrogen bonds · protein-protein
A–G · 812 Å² buried · 6 hydrogen bonds · protein-protein
F–H · 808 Å² buried · 6 hydrogen bonds · protein-protein
C–K · 802 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

3R90 · Crystal structure of Malignant T cell-amplified sequence 1 protein · the same entry in another collection · chain L against L, 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 Q9ULC4
Elsewhere: RCSB PDB 3R90 · PDBe 3R90 · UniProt Q9ULC4

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