Research workbench

S. pombe CTP1 tetramerization domain

Analyse S. pombe CTP1 tetramerization domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4X01
Type: protein
Length: 381 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA binding CTP1
EC: 3.1.-.-
UniProt: O74986

Structure

x-ray diffraction · 8 distinct chains · 89% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA binding CTP1 (EC 3.1.-.-)	protein	49	90% helix, 0% strand	O74986
B	DNA binding CTP1 (EC 3.1.-.-)	protein	49	90% helix, 0% strand	O74986
C	DNA binding CTP1 (EC 3.1.-.-)	protein	50	92% helix, 0% strand	O74986
D	DNA binding CTP1 (EC 3.1.-.-)	protein	48	85% helix, 0% strand	O74986
E	DNA binding CTP1 (EC 3.1.-.-)	protein	46	89% helix, 0% strand	O74986
F	DNA binding CTP1 (EC 3.1.-.-)	protein	47	87% helix, 0% strand	O74986
G	DNA binding CTP1 (EC 3.1.-.-)	protein	44	89% helix, 0% strand	O74986
H	DNA binding CTP1 (EC 3.1.-.-)	protein	48	90% helix, 0% strand	O74986

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 13 copies · chains A, B, D, C, G, H

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

Interfaces

12 interfaces between chains.

A–B · 1202 Å² buried · 3 hydrogen bonds · protein-protein
C–D · 1155 Å² buried · 3 hydrogen bonds · protein-protein
E–F · 1090 Å² buried · 5 hydrogen bonds · protein-protein
G–H · 1074 Å² buried · 4 hydrogen bonds · protein-protein
F–G · 442 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

4X01 · S. pombe Ctp1 tetramerization domain · the same entry in another collection · chain H against H, TM-score 1.00
O74986 · AlphaFold monomer V2.0 prediction for DNA endonuclease CTP1 (O74986) · a predicted model of the same protein · chain E against A, TM-score 0.89

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 O74986
Elsewhere: RCSB PDB 4X01 · PDBe 4X01 · UniProt O74986

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