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Adenine-specific methyltransferase M. taq I/DNA complex

Analyse Adenine-specific methyltransferase M. taq I/DNA complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1G38
Type: protein + DNA
Length: 826 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P14385

Structure

x-ray diffraction · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, E	—	dna	10	—	—
C, F	—	dna	10	—	—
A, D	—	protein	393	—	P14385

Compared structures

1G38 · Adenine-specific methyltransferase M. taq I/DNA complex · the same entry in another collection · chain C against C, TM-score 1.00
P14385 · AlphaFold monomer V2.0 prediction for modification methylase taqi (P14385) · a predicted model of the same protein · 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 P14385
Elsewhere: RCSB PDB 1G38 · PDBe 1G38 · UniProt P14385

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