1g72 Summary

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PDB entry 1g72 (supersedes 1b2n)

CATALYTIC MECHANISM OF QUINOPROTEIN METHANOL DEHYDROGENASE: A THEORETICAL AND X-RAY CRYSTALLOGRAPHIC INVESTIGATION

The structure was published by Zheng, Y.J., Xia, Z.x., Chen, Z.w., Mathews, F.S., and Bruice, T.C., in 2001 in a paper entitled "Catalytic mechanism of quinoprotein methanol dehydrogenase: A theoretical and x-ray crystallographic investigation." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 2000.

The experimental data on which the structure is based was also deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely METHANOL DEHYDROGENASE HEAVY SUBUNIT and METHANOL DEHYDROGENASE LIGHT SUBUNIT.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms heterotetramers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A METHANOL DEHYDROGENASE HEAVY SUBUNIT P38539 (1-573) (DHM1_METME)search Methylophilus methylotrophussearch 100% 573 99%
C METHANOL DEHYDROGENASE HEAVY SUBUNIT P38539 (1-573) (DHM1_METME)search Methylophilus methylotrophussearch 100% 573 99%
B METHANOL DEHYDROGENASE LIGHT SUBUNIT P38540 (23-91) (DHM2_METME)search Methylophilus methylotrophussearch 100% 69 82%
D METHANOL DEHYDROGENASE LIGHT SUBUNIT P38540 (23-91) (DHM2_METME)search Methylophilus methylotrophussearch 100% 69 82%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P38539 (1 - 573) METHANOL DEHYDROGENASE HEAVY SUBUNIT Methylophilus methylotrophus W3A1
P38540 (23 - 91) METHANOL DEHYDROGENASE LIGHT SUBUNIT Methylophilus methylotrophus W3A1

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, C (P38539) Quinoprotein alcohol dehydrogenase-likesearch Methanol Dehydrogenase; Chain Asearch PF01011: PQQ enzyme repeatsearch
B, D (P38540) Methanol dehydrogenase subunitsearch Methanol Dehydrogenase, chain Bsearch PF02315: Methanol dehydrogenase beta subunitsearch

Chain ID Cellular component (GO) Biological process (GO) Molecular function (GO)
A, C (P38539) plasma membranesearch membranesearch outer membrane-bounded periplasmic spacesearch methanol metabolic processsearch oxidation-reduction processsearch oxidoreductase activitysearch metal ion bindingsearch methanol ferricytochrome-c oxidoreductase activitysearch ethanol cytochrome-c oxidoreductase activitysearch 2-chloroethanol cytochrome-c oxidoreductase activitysearch alcohol dehydrogenase (cytochrome c(L)) activitysearch
B, D (P38540) plasma membranesearch membranesearch methanol metabolic processsearch methanol oxidationsearch oxidation-reduction processsearch alcohol dehydrogenase (NAD) activitysearch oxidoreductase activitysearch methanol ferricytochrome-c oxidoreductase activitysearch ethanol cytochrome-c oxidoreductase activitysearch 2-chloroethanol cytochrome-c oxidoreductase activitysearch alcohol dehydrogenase (cytochrome c(L)) activitysearch

Chain InterPro annotation
A, C Quinoprotein dehydrogenase, conserved sitesearch Pyrrolo-quinoline quinone repeatsearch Quinonprotein alcohol dehydrogenase-like superfamilysearch PQQ-dependent dehydrogenase, methanol/ethanol familysearch Pyrrolo-quinoline quinone beta-propeller repeatsearch Quinonprotein alcohol dehydrogenase-like domainsearch
B, D Methanol dehydrogenase, beta subunitsearch