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PDBsum entry 3ch4

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Transferase PDB id
3ch4
Contents
Protein chain
188 a.a.
Ligands
SO4 ×2
MPD ×2
Waters ×148

References listed in PDB file
Key reference
Title Crystal structure of human phosphomevalonate kinase at 1.8 a resolution.
Authors Q.Chang, X.X.Yan, S.Y.Gu, J.F.Liu, D.C.Liang.
Ref. Proteins, 2008, 73, 254-258. [DOI no: 10.1002/prot.22151]
PubMed id 18618710
Abstract
No abstract given.
Figure 1.
Figure 1. A: Stereo ribbon representation of hPMK. The different regions of the enzyme are color-coded. CORE region is shown in magenta, LID region in green, and substrate binding region in light brown. MPD (cyan) and sulfate ions (orange) are shown in stick models. The P-loop is shown in dark blue. B: Stereo ribbon representation of the superposition of DNK (deoxynucleoside monophosphate kinase from Bacteriophage T4, PDB: 1dek) with hPMK. DNK is shown in yellow and PMK in purple.
Figure 2.
Figure 2. A: A superimposed view of the ATP binding site of sulfate-bound PMK (purple), ATP-bound GntK (orange), and ATP-bound DCK (green). The superimposition is based on C atoms of the P-loop, helix 1 and strand 1. ATP, MPD and sulfate ion are shown in stick models. B: The interactions with the bounded sulfate ion and the interactions between residues located in the P-loop and LID region. The sulfate ion (SO[4]) and correlative residues are represented by stick structures, and the remainder of the structure is shown in cartoon representation. Carbon atoms are colored in purple, oxygen atoms in red, nitrogen atoms in blue and the sulfur atom is yellow. Hydrogen bond pairs are connected with green dashed lines. C: Electrostatic surface representation of hPMK with the transparent ribbon presentation. Red represents a negative charge, and blue represents a positive charge. MPD and sulfate ion are represented by sticks. The ATP-binding site is the region within the cyan ellipse, and the substrate-binding site is the region within the white rectangle. An enlarged view of the detailed putative substrate-binding site is shown on the right, and the conserved residues that may interact with mevalonate 5-phosphate are shown by stick structures.
The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2008, 73, 254-258) copyright 2008.
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