MolNFT v1 · #180221 · protein + DNA

DNA polymerase mu, DGTP:CT product state ternary complex, 10 mm MN2+ (960MIN)

7KSV: “DNA polymerase mu, DGTP:CT product state ternary complex, 10 mm MN2+ (960MIN)”. X-ray diffraction, 3 ligands (GOA, MN, NA). MolNFT v1 #180221 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7KSV
Type: protein + DNA
Length: 343 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q9NP87
Ligands: GOA, MN, NA

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	325	—	Q9NP87
T	—	dna	9	—	—
P	—	dna	5	—	—
D	—	dna	4	—	—

Ligands and binding sites

GOA · Glycolic acid · ligand · chains A, P
MN · Manganese (II) ion · metal · 6 copies · chains A, P, D, T
NA · Sodium ion · metal · chains A, P
EDO · 1,2-ethanediol · additive · 6 copies · chains A, P, T
DTT · 2,3-dihydroxy-1,4-dithiobutane · additive · 2 copies · chains A
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.

Compared structures

7KSV · DNA Polymerase Mu, dGTP:Ct Product State Ternary Complex, 10 mM Mn2+ (960min) · the same entry in another collection · chain A against A, TM-score 1.00
Q9NP87 · AlphaFold monomer V2.0 prediction for DNA-directed DNA/RNA polymerase mu (Q9NP87) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q9NP87
Elsewhere: RCSB PDB 7KSV · PDBe 7KSV · UniProt Q9NP87

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