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Internal xylan binding domain from C. fimi Xyn10A, R262G mutant
Authors
Simpson, P.J., Hefang, X., Bolam, D.N., Gilbert, H.J., Williamson, M.P.
Assembly
XYLANASE D
Entity
1. XYLANASE D (polymer, Thiol state: all disulfide bound), 87 monomers, 8684.245 Da Detail

TGCSVTATRA EEWSDGFNVT YSVSGSSAWT VNLALNGSQT IQASWNANVT GSGSTRTVTP NGSGNTFGVT VMKNGSSTTP AATCAGS


Formula weight
8684.245 Da
Entity Connection
disulfide 1 Detail

IDTypeValue orderAtom ID 1Atom ID 2
1disulfidesing1:CYS3:SG1:CYS84:SG

Source organism
Cellulomonas fimi
Exptl. method
NMR
Refine. method
HYBRID DISTANCE GEOMETRY/ SIMULATED ANNEALING
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 98.9 %, Completeness: 98.3 %, Completeness (bb): 98.1 % Detail

Polymer type: polypeptide(L)

Total1H15N
All98.3 % (519 of 528)98.1 % (422 of 430)99.0 % (97 of 98)
Backbone98.1 % (263 of 268)97.8 % (179 of 183)98.8 % (84 of 85)
Sidechain98.5 % (256 of 260)98.4 % (243 of 247)100.0 % (13 of 13)
Aromatic100.0 % (35 of 35)100.0 % (32 of 32)100.0 % (3 of 3)
Methyl95.7 % (44 of 46)95.7 % (44 of 46)

1. XYLANASE D

TGCSVTATRA EEWSDGFNVT YSVSGSSAWT VNLALNGSQT IQASWNANVT GSGSTRTVTP NGSGNTFGVT VMKNGSSTTP AATCAGS

Sample

Temperature 310 K, pH 5.0


#NameIsotope labelingTypeConcentration
1XYLANASE D[U-15N]1.5 mM

Protein Blocks Logo
Calculated from 5 models in PDB: 1E5C, Strand ID: A Detail


Release date
2000-09-06
Citation
The structural basis for the ligand specificity of family 2 carbohydrate-binding modules
Simpson, P.J., Xie, H., Bolam, D.N., Gilbert, H.J., Williamson, M.P.
J. Biol. Chem. (2000), 275, 41137-41142, PubMed 10973978 , DOI 10.1074/jbc.M006948200 ,
Related entities 1. XYLANASE D, : 1 : 1 : 3 : 14 entities Detail
Experiments performed 9 experiments Detail
nullKeywords BETA-SHEET, HYDROLASE, XYLAN BINDING DOMAIN, XYLANASE