5BYW: Engineered trifunctional CtCEL5E

Crystal structure of engineered trifunctional CtCEL5E. Determined by X-ray diffraction at 2.6 Å resolution. Released 15 Jun 2016.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)
Chains: 5
Atoms: 13,396
Mol. weight: 236.86 kDa
Released: 15 Jun 2016

Explore 5BYW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5BYW contains 85 α-helices and 60 β-strands across 5 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: 19 helices, 12 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
α-helix	140	1
β-strand	141	1	2
α-helix	142	1
α-helix	143-158	16
β-strand	162-165	4	1
α-helix	172-175	4
α-helix	177-194	18
β-strand	202-205	4	1
α-helix	216-233	18
β-strand	239-241	3	1
α-helix	244-247	4
α-helix	249-252	4
α-helix	256-258	3
β-strand	263-269	7	1
α-helix	273-276	4
α-helix	286-289	4
α-helix	297-317	21
β-strand	321-326	6	1
α-helix	334-350	17
β-strand	354-357	4	1
α-helix	366-368	3
β-strand	373-374	2	3
β-strand	379-380	2	3
α-helix	382-389	8

Chain B: 16 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	78-85	8
β-strand	87-90	4	4
α-helix	105-107	3
α-helix	110-118	9
β-strand	122-125	4	4
α-helix	130-132	3
β-strand	133	1	5
β-strand	141	1	5
α-helix	143-158	16
β-strand	162-165	4	4
α-helix	172-175	4
α-helix	177-194	18
β-strand	202-205	4	4
α-helix	216-233	18
β-strand	239-241	3	4
α-helix	244-247	4
α-helix	249-252	4
β-strand	263-268	6	4
α-helix	273-276	4
α-helix	286-289	4
α-helix	297-317	21
β-strand	321-325	5	4
α-helix	334-350	17
β-strand	354-357	4	4
α-helix	366-368	3
β-strand	373-374	2	6
β-strand	379-380	2	6
α-helix	382-389	8

Chain C: 16 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	78-85	8
β-strand	87-90	4	7
α-helix	105-107	3
α-helix	109-117	9
β-strand	122-125	4	7
α-helix	130-132	3
β-strand	133	1	8
β-strand	141	1	8
α-helix	143-158	16
β-strand	162-165	4	7
α-helix	172-175	4
α-helix	177-194	18
β-strand	202-205	4	7
α-helix	216-233	18
β-strand	239-241	3	7
α-helix	244-247	4
α-helix	249-253	5
β-strand	263-267	5	7
α-helix	273-276	4
α-helix	286-289	4
α-helix	297-316	20
β-strand	321-323	3	7
α-helix	334-350	17
β-strand	354-357	4	7
α-helix	366-368	3
β-strand	373-374	2	9
β-strand	379-380	2	9
α-helix	382-389	8

Chain D: 17 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	78-85	8
β-strand	87-90	4	10
α-helix	105-107	3
α-helix	109-118	10
β-strand	122-125	4	10
β-strand	133	1	11
α-helix	140	1
β-strand	141	1	11
α-helix	142	1
α-helix	143-158	16
β-strand	162-165	4	10
α-helix	172-175	4
α-helix	177-194	18
β-strand	202-205	4	10
α-helix	216-231	16
β-strand	239-241	3	10
α-helix	244-247	4
α-helix	249-252	4
β-strand	263-267	5	10
α-helix	273-276	4
α-helix	286-289	4
α-helix	297-316	20
β-strand	321-323	3	10
α-helix	334-350	17
β-strand	354-357	4	10
α-helix	366-368	3
β-strand	373-374	2	12
β-strand	379-380	2	12
α-helix	382-389	8

Chain E: 17 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	78-85	8
β-strand	87-90	4	13
α-helix	105-107	3
α-helix	109-117	9
β-strand	122-125	4	13
α-helix	130-132	3
β-strand	133	1	14
β-strand	141	1	14
α-helix	143-158	16
β-strand	162-165	4	13
α-helix	172-175	4
α-helix	177-194	18
β-strand	202-205	4	13
α-helix	216-233	18
β-strand	239-241	3	13
α-helix	244-247	4
α-helix	249-252	4
α-helix	256-258	3
β-strand	263-268	6	13
α-helix	273-276	4
α-helix	286-289	4
α-helix	297-316	20
β-strand	321-325	5	13
α-helix	334-349	16
β-strand	354-357	4	13
α-helix	366-368	3
β-strand	373-374	2	15
β-strand	379-380	2	15
α-helix	382-389	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Endoglucanase H	A, B, C, D, E	protein	414	Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)	P16218 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E), FASTA

>5BYW_1 Endoglucanase H (chains A, B, C, D, E)
MGSSHHHHHHSSGLVPRGSHMASMTGGQQMGRIEGREFSSPEALAAYREAIGAGSSNPTP
TPTWTSTPPSSSPKAVDPFEMVRKMGMGTNLGNTLEAPYEGSWSKSAMEYYFDDFKAAGY
KNVRIPVRWDNHTMRTYPYTIDKAFLDRVEQVVDWSLSRGFVTIINSHHDDWIKEDYNGN
IERFEKIWEQIAERFKNKSENLLFEIMNEPFGNITDEQIDDMNSRILKIIRKTNPTRIVI
IGGGYWNSYNTLVNIKIPDDPYLIGTAHYYDPFEFTHQGAEWVEGSEKWLGRKWGTQEDM
DTVVRVFDFVKSWSDRNNIPVYFGEFAVMAYADRTSRVKWYDFISDAALERGFACSVWDN
GVFGSLDNDMAIYNRDTRTFDTEILNALFNPGTYPSYSPKPSPTPRPTKPPVTP

Primary citation

Crystal structure of engineered trifunctional CtCel5E. Lin, W.L., Liang, P.H., Ho, M.C. To be published.

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…
4U3A 2.42 Å, Crystal structure of CtCel5E
4U5I 2.5 Å, Complex structure of mutant CtCel5E (E314A) with xylobiose
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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