1GKB

CONCANAVALIN A, NEW CRYSTAL FORM

Replaces:  1E0I

Summary for 1GKB

• Entry DOI: 10.2210/pdb1gkb/pdb
• Related: 1APN 1AZD 1BXH 1C57 1CES 1CJP 1CN1 1CNV 1CON 1CVN 1DGL 1DQ0 1DQ1 1DQ2 1DQ4 1DQ5 1DQ6 1ENQ 1ENR 1ENS 1GIC 1I3H 1JBC 1NLS 1ONA 1QDC 1QDO 1QGL 1QNY 1SCR 1SCS 1TEI 1VAL 1VAM 1VLN 2CNA 2CTV 2ENR 3CNA 3ENR 5CNA
• Descriptor: CONCANAVALIN A, MANGANESE (II) ION, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: lectin-binding protein
• Biological source: CANAVALIA ENSIFORMIS (JACK BEAN)
• Total number of polymer chains: 2
• Total formula weight: 51483.41

Authors

Kantardjieff, K.,Rupp, B.,Hoechtl, P.,Segelke, B. (deposition date: 2001-08-10, release date: 2001-08-20, Last modification date: 2023-12-13)

Primary citation

Kantardjieff, K.,Hochtl, P.,Segelke, B.,Tao, F.,Rupp, B.
Concanavalin a in a Dimeric Crystal Form: Revisiting Structural Accuracy and Molecular Flexibility
Acta Crystallogr.,Sect.D, 58:735-, 2002

PubMed Abstract: A structure of native concanavalin A (ConA), a hardy perennial of structural biology, has been determined in a dimeric crystal form at a resolution of 1.56 A (space group C222(1); unit-cell parameters a = 118.70, b = 101.38, c = 111.97 A; two molecules in the asymmetric unit). The structure has been refined to an R(free) of 0.206 (R = 0.178) after iterative model building and phase-bias removal using Shake&wARP. Correspondence between calculated water-tyrosine interactions and experimentally observed structures near the saccharide-binding site suggests that the observed interactions between Tyr12 and water in various crystal forms are to be expected and are not unique to the presence of an active site. The present structure differs from previously reported atomic resolution structures of ConA in several regions and extends insight into the conformational flexibility of this molecule. Furthermore, this third, low-temperature, structure of ConA in a different crystal form, independently refined using powerful model-bias removal techniques, affords the opportunity to revisit assessment of accuracy and precision in high- or atomic resolution protein structures. It is illustrated that several precise structures of the same molecule can differ substantially in local detail and users of crystallographic models are reminded to consider the potential impact when interpreting structures. Suggestions on how to effectively represent ensembles of crystallographic models of a given molecule are provided.

PubMed: 11976483
DOI: 10.1107/S0907444901019588

Experimental method

X-RAY DIFFRACTION (1.56 Å)