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1VPE

CRYSTALLOGRAPHIC ANALYSIS OF PHOSPHOGLYCERATE KINASE FROM THE HYPERTHERMOPHILIC BACTERIUM THERMOTOGA MARITIMA

Summary for 1VPE
Entry DOI10.2210/pdb1vpe/pdb
DescriptorPHOSPHOGLYCERATE KINASE, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (5 entities in total)
Functional Keywordstransferase, phosphoglycerate kinase, thermotoga maritima, hyperthermostability, crystal, amp-pnp, 3-pga
Biological sourceThermotoga maritima
Cellular locationCytoplasm: P36204
Total number of polymer chains1
Total formula weight43762.41
Authors
Auerbach, G.,Huber, R.,Graettinger, M.,Zaiss, K.,Schurig, H.,Jaenicke, R.,Jacob, U. (deposition date: 1997-05-06, release date: 1998-06-17, Last modification date: 2022-12-21)
Primary citationAuerbach, G.,Huber, R.,Grattinger, M.,Zaiss, K.,Schurig, H.,Jaenicke, R.,Jacob, U.
Closed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability.
Structure, 5:1475-1483, 1997
Cited by
PubMed: 9384563
DOI: 10.1016/S0969-2126(97)00297-9
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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