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2Q92

E. coli methionine aminopeptidase Mn-form with inhibitor B23

Summary for 2Q92
Entry DOI10.2210/pdb2q92/pdb
Related1xnz 2Q93 2Q94 2Q95 2Q96 2evc 2evm 2gtx
DescriptorMethionine aminopeptidase, MANGANESE (II) ION, SODIUM ION, ... (5 entities in total)
Functional Keywordsaminopeptidase, hydrolase, dinuclear, mn(ii)-form, enzyme-inhibitor complex, metalloenzyme
Biological sourceEscherichia coli
Total number of polymer chains1
Total formula weight29476.57
Authors
Ye, Q.-Z. (deposition date: 2007-06-12, release date: 2008-01-01, Last modification date: 2023-08-30)
Primary citationMa, Z.Q.,Xie, S.X.,Huang, Q.Q.,Nan, F.J.,Hurley, T.D.,Ye, Q.Z.
Structural analysis of inhibition of E. coli methionine aminopeptidase: implication of loop flexibility in selective inhibition of bacterial enzymes.
Bmc Struct.Biol., 7:84-84, 2007
Cited by
PubMed Abstract: Methionine aminopeptidase is a potential target of future antibacterial and anticancer drugs. Structural analysis of complexes of the enzyme with its inhibitors provides valuable information for structure-based drug design efforts.
PubMed: 18093325
DOI: 10.1186/1472-6807-7-84
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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