1jkq

X-ray diffraction
2.86Å resolution

Testing the Water-Mediated HIN Recombinase DNA Recognition by Systematic Mutations

Released:

Function and Biology Details

Reactions catalysed:
L-cystathionine + H(2)O = L-homocysteine + NH(3) + pyruvate
L-arginine + 2-oxoglutarate + O(2) = (3S)-3-hydroxy-L-arginine + succinate + CO(2)
5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP
(1a) L-cystathionine = L-cysteine + 2-aminobut-2-enoate
D-ribose 5-phosphate = D-ribulose 5-phosphate
S-adenosyl-L-methionine + a catechol = S-adenosyl-L-homocysteine + a guaiacol
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.
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.
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins
Autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly-|-Arg- and -Lys-|-Arg-.
ATP + RNA(n) = diphosphate + RNA(n+1)
5,10-methylenetetrahydrofolate + glycine + H(2)O = tetrahydrofolate + L-serine
Succinate + a quinone = fumarate + a quinol
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'.
4a-hydroxytetrahydrobiopterin = 6,7-dihydrobiopterin + H(2)O
(S)-dihydroorotate + fumarate = orotate + succinate
Selective cleavage of Tyr-|-Gly bond in picornavirus polyprotein.
10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinose = 5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinose
ATP + H(2)O = ADP + phosphate
NTP + H(2)O = NDP + phosphate
2 3-phospho-D-glycerate + 2 H(+) = D-ribulose 1,5-bisphosphate + CO(2) + H(2)O
Pyruvate + L-aspartate-4-semialdehyde = (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + H(2)O
A 5'-phosphopolynucleotide + H(2)O = a polynucleotide + phosphate
N-carbamoylputrescine + H(2)O = putrescine + CO(2) + NH(3)
(S)-malate = fumarate + H(2)O
An aldehyde + NAD(P)(+) + H(2)O = a carboxylate + NAD(P)H
ATP + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole
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.
ADP-alpha-D-glucose + D-glucose 6-phosphate = ADP + alpha,alpha-trehalose 6-phosphate
L-lysine + NADPH + O(2) = N(6)-hydroxy-L-lysine + NADP(+) + H(2)O
Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides
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.
4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O
5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH
ADP-D-ribose 1''-phosphate + H(2)O = ADP-D-ribose + phosphate
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid
A chalcone = a flavanone
The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate
ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2)
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Chorismate = prephenate
L-asparagine + H(2)O = L-aspartate + NH(3)
UDP-alpha-D-glucuronate + NAD(+) = UDP-beta-L-threo-pentapyranos-4-ulose + CO(2) + NADH
(1a) L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine
S-formylglutathione + H(2)O = glutathione + formate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct DNA molecules
Macromolecules (3 distinct):
DNA-invertase hin Chain: C
Molecule details ›
Chain: C
Length: 52 amino acids
Theoretical weight: 6.05 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Expression system: Not provided
UniProt:
  • Canonical: P03013 (Residues: 139-190; Coverage: 27%)
Gene names: STM2772, hin
Sequence domains: Helix-turn-helix domain of resolvase
Structure domains: Homeodomain-like
5'-D(*TP*GP*TP*TP*TP*TP*TP*TP*AP*TP*AP*AP*GP*A)-3' Chain: A
Molecule details ›
Chain: A
Length: 14 nucleotides
Theoretical weight: 4.3 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Expression system: Not provided
5'-D(*AP*TP*CP*TP*TP*AP*TP*AP*AP*AP*AP*AP*AP*C)-3' Chain: B
Molecule details ›
Chain: B
Length: 14 nucleotides
Theoretical weight: 4.26 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: C2221
Unit cell:
a: 85.158Å b: 82.656Å c: 45.124Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.256 0.256 0.328
Expression system: Not provided