2CIP: Michaelis complex of a family 26 lichenase

Name: PDB 2CIP: Structure of the Michaelis complex of a family 26 lichenase
Published: 2006-07-12
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: hydrolase

Structure of the Michaelis complex of a family 26 lichenase. Determined by X-ray diffraction at 1.4 Å resolution. Released 12 Jul 2006.

Method: X-ray diffraction
Resolution: 1.4 Å
Organism: CLOSTRIDIUM THERMOCELLUM
Chains: 1
Atoms: 2,812
Mol. weight: 32.62 kDa
Ligands: ZZ1
Released: 12 Jul 2006

Explore 2CIP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2CIP contains 10 α-helices and 13 β-strands across 1 chain. 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: 10 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	8-9	2
β-strand	10-14	5	1
α-helix	21-31	11
β-strand	37-43	7	1
α-helix	48-60	13
β-strand	64-70	7	1
α-helix	76-80	5
α-helix	85-98	14
β-strand	102-106	5	1
α-helix	128-144	17
β-strand	150-152	3	1
β-strand	153	1	2
β-strand	156-157	2	1
α-helix	174-176	3
β-strand	179	1	2
β-strand	180-186	7	1
α-helix	200-211	12
β-strand	218-225	8	1
α-helix	232-246	15
β-strand	250-256	7	1
β-strand	259	1	3
β-strand	263	1	3
α-helix	270-280	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Endoglucanase H	A	protein	282	CLOSTRIDIUM THERMOCELLUM	P16218 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2CIP_1 ENDOGLUCANASE H (chains A)
MASNYNSGLKIGAWVGTQPSESAIKSFQELQGRKLDIVHQFINWSTDFSWVRPYADAVYN
NGSILMITWEPWEYNTVDIKNGKADAYITRMAQDMKAYGKEIWLRPLHEANGDWYPWAIG
YSSRVNTNETYIAAFRHIVDIFRANGATNVKWVFNVNCDNVGNGTSYLGHYPGDNYVDYT
SIDGYNWGTTQSWGSQWQSFDQVFSRAYQALASINKPIIIAQFASAEIGGNKARWITEAY
NSIRTSYNKVIAAVWFHENKETDWRINSSPEALAAYREAIGA

Ligands and cofactors

ID	Name	Formula	Copies
ZZ1	4-methyl-2H-chromen-2-one	C10 H8 O2	1

Primary citation

Substrate Distortion by a Lichenase Highlights the Different Conformational Itineraries Harnessed by Related Glycoside Hydrolases. Money, V.A., Smith, N.L., Scaffidi, A. et al. Angew Chem Int Ed Engl (2006) 45:5136. DOI 10.1002/ANIE.200600802 · 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
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
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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