1TE1
Crystal structure of family 11 xylanase in complex with inhibitor (XIP-I)
- PDB DOI: https://doi.org/10.2210/pdb1TE1/pdb
- Classification: HYDROLASE INHIBITOR/HYDROLASE
- Organism(s): Triticum aestivum, Talaromyces funiculosus
- Expression System: Talaromyces funiculosus
- Mutation(s): No
- Deposited: 2004-05-24 Released: 2004-07-20
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.50 Å
- R-Value Free: 0.271
- R-Value Work: 0.208
- R-Value Observed: 0.213
This is version 1.4 of the entry. See complete history.
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| xylanase inhibitor protein I | 274 | Triticum aestivum | Mutation(s): 0 |  | |
UniProt | |||||
Find proteins for Q8L5C6 (Triticum aestivum) Explore Q8L5C6 Go to UniProtKB: Q8L5C6 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q8L5C6 | ||||
Sequence AnnotationsExpand | |||||
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Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| endo-1,4-xylanase | 190 | Talaromyces funiculosus | Mutation(s): 0 Gene Names: xynC EC: 3.2.1.8 |  | |
UniProt | |||||
Find proteins for Q9HFH0 (Talaromyces funiculosus) Explore Q9HFH0 Go to UniProtKB: Q9HFH0 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q9HFH0 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| NAG Query on NAG | C [auth A], D [auth A] | 2-acetamido-2-deoxy-beta-D-glucopyranose C8 H15 N O6 OVRNDRQMDRJTHS-FMDGEEDCSA-N |  | ||
| EDO Query on EDO | E [auth A] F [auth A] G [auth A] H [auth A] I [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.50 Å
- R-Value Free: 0.271
- R-Value Work: 0.208
- R-Value Observed: 0.213
- Space Group: P 43 21 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 98.748 | α = 90 |
| b = 98.748 | β = 90 |
| c = 112.095 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| MOSFLM | data reduction |
| CCP4 | data scaling |
| AMoRE | phasing |
Entry History
Deposition Data
- Released Date: 2004-07-20 Deposition Author(s): Payan, F., Leone, P., Furniss, C., Tahir, T., Durand, A., Porciero, S., Manzanares, P., Williamson, G., Gilbert, H.J., Juge, N., Roussel, A.
Revision History (Full details and data files)
- Version 1.0: 2004-07-20
Type: Initial release - Version 1.1: 2008-04-30
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Non-polymer description, Version format compliance - Version 1.3: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Advisory, Data collection, Derived calculations, Structure summary - Version 1.4: 2023-08-23
Changes: Data collection, Database references, Refinement description, Structure summary
