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PDBsum entry 3ilo

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Top Page protein ligands metals links
Transferase PDB id
3ilo
Contents
Protein chain
158 a.a.
Ligands
APC
PH2
ACT
Metals
_MG
_CL
Waters ×385

References listed in PDB file
Key reference
Title Structural and functional roles of residues d95 and d e. Coli hppk
Authors Y.Li, J.Blaszczyk, X.Ji, H.Yan.
Ref. TO BE PUBLISHED ...
Secondary reference #1
Title Catalytic center assembly of hppk as revealed by the crystal structure of a ternary complex at 1.25 a resolution.
Authors J.Blaszczyk, G.Shi, H.Yan, X.Ji.
Ref. Structure, 2000, 8, 1049-1058. [DOI no: 10.1016/S0969-2126(00)00502-5]
PubMed id 11080626
Full text Abstract
Figure 4.
Figure 4. The Open and Closed Catalytic Center of HPPK(a) The three uncoupled flexible loops of HPPK in the apo-enzyme [2].(b) The coupling of these loops in the ternary complex. In the ternary complex, a hydrogen-bond network involves N10 from Loop-1; P47 and Q50 from Loop-2; and W89, P91, and R92 from Loop-3. This network is not observed in apo-HPPK. The orientation of the drawing is indicated by the position of the substrate molecules HP and MgAMPCPP. (This figure was prepared with the program MOLSCRIPT [21].)

The above figure is reproduced from the cited reference with permission from Cell Press
PROCHECK
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