1dii Summary

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CRYSTAL STRUCTURE OF P-CRESOL METHYLHYDROXYLASE AT 2.5 A RESOLUTION

The structure was published by Cunane, L.M., Chen, Z.W., Shamala, N., Mathews, F.S., Cronin, C.N., and McIntire, W.S., in 2000 in a paper entitled "Structures of the flavocytochrome p-cresol methylhydroxylase and its enzyme-substrate complex: gated substrate entry and proton relays support the proposed catalytic mechanism." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 1999.

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

This PDB entry contains a complex of 2 biomacromolecules, namely P-CRESOL METHYLHYDROXYLASE.

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 P-CRESOL METHYLHYDROXYLASE P09788 (1-521) (DH4C_PSEPU)search Pseudomonas putidasearch 100% 521 98%
B P-CRESOL METHYLHYDROXYLASE P09788 (1-521) (DH4C_PSEPU)search Pseudomonas putidasearch 100% 521 98%
C P-CRESOL METHYLHYDROXYLASE P09787 (34-113) (CY4C_PSEPU)search Pseudomonas putidasearch 100% 80 91%
D P-CRESOL METHYLHYDROXYLASE P09787 (34-113) (CY4C_PSEPU)search Pseudomonas putidasearch 100% 80 91%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P09788 (1 - 521) P-CRESOL METHYLHYDROXYLASE Pseudomonas putida
P09787 (34 - 113) P-CRESOL METHYLHYDROXYLASE Pseudomonas putida

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P09788) Vanillyl-alcohol oxidase-likesearch, FAD-linked oxidases, N-terminal domainsearch Vanillyl-alcohol Oxidase; Chain A, domain 3search, Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2search, Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3search, Vanillyl-alcohol Oxidase; Chain A, domain 4search PF01565: FAD binding domainsearch, PF02913: FAD linked oxidases, C-terminal domainsearch
C, D (P09787) monodomain cytochrome csearch Cytochrome csearch PF13442: Cytochrome C oxidase, cbb3-type, subunit IIIsearch

Chain ID Biological process (GO) Molecular function (GO)
A, B (P09788) oxidation-reduction processsearch flavin adenine dinucleotide bindingsearch oxidoreductase activitysearch oxidoreductase activity, acting on CH-OH group of donorssearch catalytic activitysearch UDP-N-acetylmuramate dehydrogenase activitysearch 4-cresol dehydrogenase (hydroxylating) activitysearch
C, D (P09787) oxidation-reduction processsearch heme bindingsearch electron carrier activitysearch metal ion bindingsearch

Chain InterPro annotation
A, B FAD-linked oxidase, C-terminalsearch FAD linked oxidase, N-terminalsearch FAD-linked oxidase-like, C-terminalsearch FAD-binding, type 2search FAD-binding, type 2, subdomain 1search CO dehydrogenase flavoprotein-like, FAD-binding, subdomain 2search Vanillyl-alcohol oxidase/Cytokinin dehydrogenase C-terminal domainsearch Vanillyl-alcohol oxidase, C-terminal subdomain 2search
C, D Cytochrome c-like domainsearch