MolNFT v1 · #48738 · protein + DNA

Structure of nucleic-acid binding protein

2Q2K · DNA (5'-D(*AP*GP*TP*AP*TP*AP*(5IU)P*AP*CP*(5IU)…: “Structure of nucleic-acid binding protein”. X-ray diffraction. MolNFT v1 #48738 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2Q2K
Type: protein + DNA
Length: 109 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA (5'-D(*AP*GP*TP*AP*TP*AP*(5IU)P*AP*CP*(5IU) P*AP*GP*TP*AP*TP*AP*TP*AP*CP*T)-3')…
UniProt: Q2FDA3

Structure

x-ray diffraction · 3 distinct chains · 51% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
F	DNA (5'-D(APGPTPAPTPAP(5IU)PAPCP(5IU) PAPGPTPAPTPAPTPAPCPT)-3')	dna	20	—	—
A	Hypothetical protein	protein	45	49% helix, 20% strand	Q2FDA3
B	Hypothetical protein	protein	44	52% helix, 20% strand	Q2FDA3

Ligands and binding sites

EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A

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

Interfaces

3 interfaces between chains.

A–B · 1979 Å² buried · 21 hydrogen bonds · protein-protein
F–A · 314 Å² buried · 9 hydrogen bonds · protein-nucleic
F–B · 288 Å² buried · 5 hydrogen bonds · protein-nucleic

Modifications

Observed in the structure: 2 modified (nucleotide modification).

Compared structures

2Q2K · Structure of nucleic-acid binding protein · the same entry in another collection · chain F against F, 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 Q2FDA3
Elsewhere: RCSB PDB 2Q2K · PDBe 2Q2K · UniProt Q2FDA3

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