4U3A: CtCel5E

Crystal structure of CtCel5E. Determined by X-ray diffraction at 2.42 Å resolution. Released 14 Jan 2015.

Method: X-ray diffraction
Resolution: 2.42 Å
Organism: Clostridium thermocellum ATCC 27405
Chains: 2
Atoms: 4,930
Mol. weight: 92.5 kDa
Released: 14 Jan 2015

Explore 4U3A in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4U3A contains 23 α-helices and 32 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 11 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	78-85	8
β-strand	87-90	4	1
α-helix	105-107	3
α-helix	109-118	10
β-strand	122-125	4	1
α-helix	130-132	3
β-strand	133	1	2
β-strand	141	1	2
α-helix	143-158	16
β-strand	162-166	5	1
α-helix	172-175	4
α-helix	177-194	18
β-strand	202-205	4	1
β-strand	212	1	3
β-strand	214	1	3
α-helix	216-233	18
β-strand	239-246	8	1
β-strand	251-253	3	1
β-strand	263-269	7	1
β-strand	283	1	4
α-helix	286-306	21
β-strand	310-315	6	1
β-strand	320	1	4
α-helix	323-339	17
β-strand	343-346	4	1
β-strand	362-363	2	5
β-strand	368-369	2	5
α-helix	371-377	7

Chain B: 12 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	78-85	8
β-strand	87-90	4	6
α-helix	109-118	10
β-strand	122-125	4	6
α-helix	130-132	3
β-strand	133	1	7
α-helix	140	1
β-strand	141	1	7
α-helix	142	1
α-helix	143-158	16
β-strand	162-166	5	6
α-helix	172-175	4
α-helix	177-194	18
β-strand	202-205	4	6
β-strand	212	1	8
β-strand	214	1	8
α-helix	216-233	18
β-strand	239-246	8	6
β-strand	251-253	3	6
β-strand	263-269	7	6
α-helix	288-306	19
β-strand	310-315	6	6
α-helix	323-339	17
β-strand	343-346	4	6
β-strand	362-363	2	9
β-strand	368-369	2	9
α-helix	371-377	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Endoglucanase H	A, B	protein	403	Clostridium thermocellum ATCC 27405	P16218 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4U3A_1 Endoglucanase H (chains A, B)
MGSSHHHHHHSSGLVPRGSHMASMTGGQQMGRIEGREFSSPEALAAYREAIGAGSSNPTP
TPTWTSTPPSSSPKAVDPFEMVRKMGMGTNLGNTLEAPYEGSWSKSAMEYYFDDFKAAGY
KNVRIPVRWDNHTMRTYPYTIDKAFLDRVEQVVDWSLSRGFVTIINSHHDDWIKEDYNGN
IERFEKIWEQIAERFKNKSENLLFEIMNEPFGNITDEQIDDMNSRILKIIRKTNPTRIVI
IGGGYWNSYNTLVNIKIPDDPYLIGTFHYYDPYEFTHKWRGTWGTQEDMDTVVRVFDFVK
SWSDRNNIPVYFGEFAVMAYADRTSRVKWYDFISDAALERGFACSVWDNGVFGSLDNDMA
IYNRDTRTFDTEILNALFNPGTYPSYSPKPSPTPRPTKPPVTP

Primary citation

Biochemical Characterization and Structural Analysis of a Bifunctional Cellulase/Xylanase from Clostridium thermocellum. Yuan, S.F., Wu, T.H., Lee, H.L. et al. J Biol Chem (2015) 290:5739-5748. DOI 10.1074/jbc.M114.604454 · PubMed

Other PDB entries of the same protein (UniProt P16218 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2V3G 1.2 Å, Structure of a family 26 lichenase in complex with noeuromycin
2CIP 1.4 Å, Structure of the Michaelis complex of a family 26 lichenase
2CIT 1.4 Å, Structure of the covalent intermediate of a family 26 lichenase
6R3M 1.45 Å, Family 11 Carbohydrate-Binding Module from Clostridium thermocellum in complex with…
2BV9 1.5 Å, How family 26 glycoside hydrolases orchestrate catalysis on different polysaccharides.…
2VI0 1.51 Å, Lichenase CtLic26 in complex with a thio-oligosaccharide
2BVD 1.6 Å, How family 26 glycoside hydrolases orchestrate catalysis on different polysaccharides.…
1V0A 1.98 Å, Family 11 Carbohydrate-Binding Module of cellulosomal cellulase Lic26A-Cel5E of…
4U5I 2.5 Å, Complex structure of mutant CtCel5E (E314A) with xylobiose
5BYW 2.6 Å, Crystal structure of engineered trifunctional CtCEL5E
6R31 2.6 Å, Family 11 Carbohydrate-Binding Module from Clostridium thermocellum in complex with…
4U5K 2.65 Å, Complex structure of mutant CtCel5E (E314A) with cellobiose

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