PDBsum entry 1a27

Dehydrogenase

PDB id: 1a27

Contents

Protein chain

285 a.a. *

Ligands

EST

NAP

Waters ×157

* Residue conservation analysis

PDB id:

1a27

Name:

Dehydrogenase

Title:

Human 17-beta-hydroxysteroid-dehydrogenase type 1 c-terminal deletion mutant complexed with estradiol and NADP+

Structure:

17-beta-hydroxysteroid-dehydrogenase. Chain: a. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Cell_line: spodoptera frugiperda. Cellular_location: cytoplasm. Expressed in: unidentified baculovirus. Expression_system_taxid: 10469. Expression_system_cell_line: spodoptera frugiperda.

Biol. unit:

Homo-Dimer (from PDB file)

Resolution:

1.90Å R-factor: 0.210 R-free: 0.261

Authors:

C.Mazza,R.Breton,D.Housset,J.-C.Fontecilla-Camps

Key ref:

S.Jung et al. (1994). Crystallization and X-ray crystallographic analysis of recombinant chicken poly(ADP-ribose) polymerase catalytic domain produced in Sf9 insect cells. J Mol Biol, 244, 114-116. PubMed id: 7966315

Date:

16-Jan-98 Release date: 27-May-98

Protein chain

P14061  (DHB1_HUMAN) -  17-beta-hydroxysteroid dehydrogenase type 1 from Homo sapiens

Seq: 328 a.a.

Struc: 285 a.a.

Enzyme reactions

• Enzyme class 1: E.C.1.1.1.51 - 3(or 17)beta-hydroxysteroid dehydrogenase.
• Reaction:
  1. testosterone + NAD⁺ = androst-4-ene-3,17-dione + NADH + H⁺
  2. testosterone + NADP⁺ = androst-4-ene-3,17-dione + NADPH + H⁺

testosterone (Bound ligand (Het Group name = NAP) matches with 91.67% similarity) + NAD(+) (Bound ligand (Het Group name = EST) matches with 95.24% similarity) = androst-4-ene-3,17-dione + NADH + H(+)

testosterone (Bound ligand (Het Group name = NAP) corresponds exactly) + NADP(+) (Bound ligand (Het Group name = EST) matches with 95.24% similarity) = androst-4-ene-3,17-dione + NADPH + H(+)

• Enzyme class 2: E.C.1.1.1.62 - 17beta-estradiol 17-dehydrogenase.
• Reaction:
  1. 17beta-estradiol + NAD⁺ = estrone + NADH + H⁺
  2. 17beta-estradiol + NADP⁺ = estrone + NADPH + H⁺

17beta-estradiol + NAD(+) (Bound ligand (Het Group name = NAP) matches with 91.67% similarity) = estrone (Bound ligand (Het Group name = EST) corresponds exactly) + NADH + H(+)

17beta-estradiol + NADP(+) (Bound ligand (Het Group name = NAP) corresponds exactly) = estrone (Bound ligand (Het Group name = EST) corresponds exactly) + NADPH + H(+)

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

J Mol Biol 244:114-116 (1994)

PubMed id: 7966315

Crystallization and X-ray crystallographic analysis of recombinant chicken poly(ADP-ribose) polymerase catalytic domain produced in Sf9 insect cells.

S.Jung, E.A.Miranda, J.M.de Murcia, C.Niedergang, M.Delarue, G.E.Schulz, G.M.de Murcia.

ABSTRACT

Poly (ADP-ribose) polymerase (PARP) participates in the immediate response in mammalian cells exposed to DNA-damaging agents. Recombinant baculovirus harboring the cDNA of the chicken PARP catalytic domain (40 kDa) have been used to infect Spodoptera frugiperda (Sf9) insect cells. The recombinant polypeptide (30 mg per 1 x 10(9) cells) was purified to homogeneity by 3-aminobenzamide affinity chromatography. The enzymatic properties of the recombinant domain were similar to those of the native fragment. Crystals of the purified recombinant catalytic domain were grown by vapor diffusion. The crystals belong to space group P2(1)2(1)2(1) with unit cell dimensions of a = 59.2 A, b = 65.0 A, c = 96.9 A. They are suitable for X-ray analysis and diffract to 2.0 A.