4OCV
N-acetylhexosamine 1-phosphate kinase_ATCC15697 in complex with GlcNAc and AMPPNP
- PDB DOI: https://doi.org/10.2210/pdb4OCV/pdb
- Classification: TRANSFERASE
- Organism(s): Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2014-01-09 Released: 2014-05-14
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.47 Å
- R-Value Free: 0.200
- R-Value Work: 0.187
- R-Value Observed: 0.188
This is version 2.1 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 |
| N-acetylhexosamine 1-phosphate kinase | 379 | Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088 | Mutation(s): 0 Gene Names: BLIJ_2250, Blon_2173 EC: 2.7.1.162 |  | |
UniProt | |||||
Find proteins for B7GN78 (Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12)) Explore B7GN78 Go to UniProtKB: B7GN78 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | B7GN78 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| ANP Query on ANP | C [auth A] | PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER C10 H17 N6 O12 P3 PVKSNHVPLWYQGJ-KQYNXXCUSA-N |  | ||
| NDG Query on NDG | B [auth A] | 2-acetamido-2-deoxy-alpha-D-glucopyranose C8 H15 N O6 OVRNDRQMDRJTHS-PVFLNQBWSA-N |  | ||
| SO4 Query on SO4 | D [auth A], E [auth A], F [auth A], G [auth A] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.47 Å
- R-Value Free: 0.200
- R-Value Work: 0.187
- R-Value Observed: 0.188
- Space Group: P 41 21 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 73.238 | α = 90 |
| b = 73.238 | β = 90 |
| c = 166.613 | γ = 90 |
| Software Name | Purpose |
|---|---|
| HKL-2000 | data collection |
| PHASER | phasing |
| REFMAC | refinement |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
Entry History
Deposition Data
- Released Date: 2014-05-14 Deposition Author(s): Li, T.L., Wang, K.C., Lyu, S.Y., Liu, Y.C., Chang, C.Y., Wu, C.J.
Revision History (Full details and data files)
- Version 1.0: 2014-05-14
Type: Initial release - Version 1.1: 2014-09-24
Changes: Database references - Version 2.0: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Atomic model, Data collection, Database references, Derived calculations, Structure summary - Version 2.1: 2023-09-20
Changes: Data collection, Database references, Refinement description, Structure summary
