PDBsum entry 1con

Lectin(agglutinin)

PDB id

1con

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Contents

			Protein chain

					237 a.a. *

			Metals

					_CD ×2


					_CA

			Waters ×144

* Residue conservation analysis

PDB id:

1con

Links

Name:

Lectin(agglutinin)

Title:

The refined structure of cadmium substituted concanavalin a at 2.0 angstroms resolution

Structure:

Concanavalin a. Chain: a. Engineered: yes

Source:

Canavalia ensiformis. Jack bean. Organism_taxid: 3823. Organ: bean

Biol. unit:

Tetramer (from PQS)

Resolution:

2.00Å

R-factor:

0.171

Authors:

J.H.Naismith,J.Habash,S.J.Harrop,J.R.Helliwell,W.N.Hunter, A.J.Kalb(gilboa),J.Yariv,T.C.M.Wan,S.Weisgerber

Key ref:

J.H.Naismith et al. (1993). Refined structure of cadmium-substituted concanavalin A at 2.0 A resolution. Acta Crystallogr D Biol Crystallogr, 49, 561-571. PubMed id: 15299493 DOI: 10.1107/S0907444993006390

Date:

16-Mar-93

Release date:

31-Jan-94

PROCHECK

	Headers

	References

Protein chain

P02866 (CONA_CANEN) - Concanavalin-A from Canavalia ensiformis

Seq: Struc:					290 a.a. 237 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 26 residue positions (black crosses)



		Enzyme reactions

Enzyme class:

E.C.?

[IntEnz] [ExPASy] [KEGG] [BRENDA]

DOI no: 10.1107/S0907444993006390	Acta Crystallogr D Biol Crystallogr 49:561-571 (1993)
PubMed id: 15299493

Refined structure of cadmium-substituted concanavalin A at 2.0 A resolution.
J.H.Naismith, J.Habash, S.Harrop, J.R.Helliwell, W.N.Hunter, T.C.Wan, S.Weisgerber, A.J.Kalb, J.Yariv.

ABSTRACT

The three-dimensional structure of cadmium-substituted concanavalin A has been refined using X-PLOR. The R factor on all data between 8 and 2 A is 17.1%. The protein crystallizes in space group I222 with cell dimensions a = 88.7, b = 86.5 and c = 62.5 A and has one protein subunit per asymmetric unit. The final structure contains 237 amino acids, two Cd ions, one Ca ion and 144 water molecules. One Cd ion occupies the transition-metal binding site and the second occupies an additional site, the coordinates of which were first reported by Weinzierl & Kalb [FEBS Lett. (1971), 18, 268-270]. The additional Cd ion is bound with distorted octahedral symmetry and bridges the cleft between the two monomers which form the conventional dimer of concanavalin A. This study provides a detailed analysis of the refined structure of saccharide-free concanavalin A and is the basis for comparison with saccharide complexes reported elsewhere.

Selected figure(s)



	Figure 5. Fig. 5. The tetramer of concanavalin A viewed down a molecular twofold axis.		Figure 6. Fig. 6. The S1 (Ca 2+) and $2 (Cd 2+) metal sites. Both sites have octahedral-like geometry with Aspl0 capping an axial position of the Ca 2� ion. Aspl9 and Aspl0 are bound to both metals. Asp208 is shown and it makes hydrogen bonds with WC which are thought to stabilize the cis peptide. The two metal ions are separated by 4.18/~,.

Figures were selected by an automated process.

Literature references that cite this PDB file's key reference

PubMed id

Reference

15525703

M.P.Blakeley, A.J.Kalb, J.R.Helliwell, and D.A.Myles (2004).
The 15-K neutron structure of saccharide-free concanavalin A.

Proc Natl Acad Sci U S A, 101, 16405-16410.

8663112

J.Bouckaert, F.Poortmans, L.Wyns, and R.Loris (1996).
Sequential structural changes upon zinc and calcium binding to metal-free concanavalin A.

J Biol Chem, 271, 16144-16150.

PDB codes:

1ces 1enq 1enr 1ens

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.