2a79

X-ray diffraction
2.9Å resolution

Mammalian Shaker Kv1.2 potassium channel- beta subunit complex

Released:
Source organism: Rattus norvegicus

Function and Biology Details

Reactions catalysed:
L-alanine = D-alanine
2-dehydro-3-deoxy-6-phosphate-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate
Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-Casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.
[Protein]-N(pi)-phospho-L-histidine + galactitol(Side 1) = [protein]-L-histidine + galactitol 1-phosphate(Side 2)
ATP + [biotin carboxyl-carrier protein]-biotin-N(6)-L-lysine + hydrogencarbonate- = ADP + phosphate + [biotin carboxyl-carrier protein]-carboxybiotin-N(6)-L-lysine
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'.
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate
TSAVLQ-|-SGFRK-NH(2) and SGVTFQ-|-GKFKK the two peptides corresponding to the two self-cleavage sites of the SARS 3C-like proteinase are the two most reactive peptide substrates. The enzyme exhibits a strong preference for substrates containing Gln at P1 position and Leu at P2 position.
ATP + glycerol = ADP + sn-glycerol 3-phosphate
ATP + pyridoxal = ADP + pyridoxal 5'-phosphate
ATP + H(2)O = ADP + phosphate
UDP-N-acetyl-alpha-D-glucosamine = UDP-2-acetamido-2,6-dideoxy-alpha-D-xylo-hex-4-ulose + H(2)O
Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier-protein]
Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
Selective cleavage of Tyr-|-Gly bond in picornavirus polyprotein.
An acyl-[acyl-carrier protein] + NAD(+) = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH
(R)-propane-1,2-diol + NAD(+) = (R)-lactaldehyde + NADH
4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate
NTP + H(2)O = NDP + phosphate
ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2)
Cellobiose = 4-O-beta-D-glucopyranosyl-D-mannose
ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr)
(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O
ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate + malonyl-CoA
Succinate semialdehyde + NAD(P)(+) + H(2)O = succinate + NAD(P)H
ATP + propanoyl-CoA + HCO(3)(-) = ADP + phosphate + (S)-methylmalonyl-CoA
ATP + H(2)O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide
Maltose = alpha,alpha-trehalose
A short-chain (3S)-3-hydroxyacyl-CoA = a short-chain trans-2-enoyl-CoA + H(2)O
Exolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan, from either the reducing or the non-reducing ends of the peptidoglycan chains, with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.
ATP + thymidine = ADP + thymidine 5'-phosphate
4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Preferential cleavage at the carboxyl of hydrophobic amino acids, but fails to cleave 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17 and 24-Phe-|-Phe-25 of insulin B chain. Activates trypsinogen, and degrades keratin.
Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and similar substrates, releasing cellobiose from the reducing ends of the chains.
S-formylglutathione + H(2)O = glutathione + formate
Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine
5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH
5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP
7,8-dihydroneopterin 3'-triphosphate + H(2)O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + triphosphate
RX + glutathione = HX + R-S-glutathione
L-glutamate + H(2)O + NADP(+) = 2-oxoglutarate + NH(3) + NADPH
Purine deoxynucleoside + phosphate = purine + 2'-deoxy-alpha-D-ribose 1-phosphate
5,10-methylenetetrahydrofolate + glycine + H(2)O = tetrahydrofolate + L-serine
Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains
ATP + a protein = ADP + a phosphoprotein
ATP + H(2)O + cellular protein(Side 1) = ADP + phosphate + cellular protein(Side 2)
An aldehyde + NAD(+) + H(2)O = a carboxylate + NADH
L-fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde
Succinate + a quinone = fumarate + a quinol
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units
1-haloalkane + H(2)O = a primary alcohol + halide
N-carbamoylputrescine + H(2)O = putrescine + CO(2) + NH(3)
L-lysine + NADPH + O(2) = N(6)-hydroxy-L-lysine + NADP(+) + H(2)O
Peptidylproline (omega=180) = peptidylproline (omega=0)
(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH
Aceneneuramate = N-acetyl-D-mannosamine + pyruvate
ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamate 5-phosphate
Chorismate = prephenate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero hexadecamer (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Voltage-gated potassium channel subunit beta-2 Chain: A
Molecule details ›
Chain: A
Length: 333 amino acids
Theoretical weight: 37.35 KDa
Source organism: Rattus norvegicus
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P62483 (Residues: 36-367; Coverage: 91%)
Gene names: Ckbeta2, Kcnab2, Kcnb3
Sequence domains: Aldo/keto reductase family
Structure domains: NADP-dependent oxidoreductase domain
Potassium voltage-gated channel subfamily A member 2 Chain: B
Molecule details ›
Chain: B
Length: 499 amino acids
Theoretical weight: 56.75 KDa
Source organism: Rattus norvegicus
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P63142 (Residues: 1-499; Coverage: 100%)
Gene name: Kcna2
Sequence domains:
Structure domains:
poly-unknown chain Chain: C
Molecule details ›
Chain: C
Length: 52 amino acids
Theoretical weight: 4.44 KDa
Source organism: Rattus norvegicus
Expression system: Komagataella pastoris
poly-unknown chain Chain: D
Molecule details ›
Chain: D
Length: 21 amino acids
Theoretical weight: 1.81 KDa
Source organism: Rattus norvegicus
Expression system: Komagataella pastoris

Ligands and Environments


Cofactor: Ligand NAP 1 x NAP
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: I4
Unit cell:
a: 113.605Å b: 113.605Å c: 260.473Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.222 0.252
Expression system: Komagataella pastoris