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InterPro: IPR003610 Carbohydrate-binding domain, family 5/12

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1242 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession List
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Accession

IPR003610 Carb-bd_dom_fam5/12

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF02839	CBM_5_12	1206
SMART	SM00495	ChtBD3	1038
SuperFamily	SSF51055	CBM_5_12	1130
Signatures in BioMart

GO Term annotation Help

Process

GO:0005975 carbohydrate metabolic process

Function

GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0030246 carbohydrate binding

Component

GO:0005576 extracellular region

InterPro annotation

Entry Details in BioMart

Abstract

The carbohydrate-binding domain (CBD) is a short domain found in many different glycosyl hydrolase enzymes, such as the C-terminal cellulose-binding domain of endoglucanase Z [1]. The domain has a core structure consisting of a 3-stranded meander beta-sheet, which contains six aromatic groups that may be important for binding.

The overall topology of the CBD is structurally similar to the C-terminal chitin-binding domains (ChBD) of chitinase A1 and chitinase B, however the binding mechanism for the ChBD may be different from that of the CBD [2].

Structural links Help

PDB - click here

SCOP: b.72.2.1

CATH: 2.10.10.20

Database links Help

Enzyme: EC:3

PANDIT: PF02839

Blocks: IPB003610

Taxonomic coverage Help

Example proteins Help

O85465 Endoglucanase 5A

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013781	Glycoside hydrolase, subgroup, catalytic core
IPR001547	Glycoside hydrolase, family 5
IPR003610	Carbohydrate-binding domain, family 5/12
IPR017853	Glycoside hydrolase, catalytic core
IPR018087	Glycoside hydrolase, family 5, conserved site
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Brun E, Moriaud F, Gans P, Blackledge MJ, Barras F, Marion D. Solution structure of the cellulose-binding domain of the endoglucanase Z secreted by Erwinia chrysanthemi. Biochemistry 36 16074-86 1997 [PubMed: 9405041] http://dx.doi.org/10.1021/bi9718494
2.	Ikegami T, Okada T, Hashimoto M, Seino S, Watanabe T, Shirakawa M. Solution structure of the chitin-binding domain of Bacillus circulans WL-12 chitinase A1. J. Biol. Chem. 275 13654-61 2000 [PubMed: 10788483] http://dx.doi.org/10.1074/jbc.275.18.13654

Additional Reading Open in usermanual
	Vaaje-Kolstad G, Vasella A, Peter MG, Netter C, Houston DR, Westereng B, Synstad B, Eijsink VG, van Aalten DM. Interactions of a family 18 chitinase with the designed inhibitor HM508 and its degradation product, chitobiono-delta-lactone. J. Biol. Chem. 279 2004 3612-9 [PubMed: 14597613] http://dx.doi.org/10.1074/jbc.M310057200
	Houston DR, Eggleston I, Synstad B, Eijsink VG, van Aalten DM. The cyclic dipeptide CI-4 [cyclo-(l-Arg-d-Pro)] inhibits family 18 chitinases by structural mimicry of a reaction intermediate. Biochem. J. 368 2002 23-7 [PubMed: 12323074] http://dx.doi.org/10.1042/BJ20021034
	Kolstad G, Synstad B, Eijsink VG, van Aalten DM. Structure of the D140N mutant of chitinase B from Serratia marcescens at 1.45 A resolution. Acta Crystallogr. D Biol. Crystallogr. 58 2002 377-9 [PubMed: 11807282] http://dx.doi.org/10.1107/S0907444901018972
	Houston DR, Shiomi K, Arai N, Omura S, Peter MG, Turberg A, Synstad B, Eijsink VG, van Aalten DM. High-resolution structures of a chitinase complexed with natural product cyclopentapeptide inhibitors: mimicry of carbohydrate substrate. Proc. Natl. Acad. Sci. U.S.A. 99 2002 9127-32 [PubMed: 12093900] http://dx.doi.org/10.1073/pnas.132060599
	Vaaje-Kolstad G, Houston DR, Rao FV, Peter MG, Synstad B, van Aalten DM, Eijsink VG. Structure of the D142N mutant of the family 18 chitinase ChiB from Serratia marcescens and its complex with allosamidin. Biochim. Biophys. Acta 1696 2004 103-11 [PubMed: 14726210]

InterPro 23.1