1R55
Crystal structure of the catalytic domain of human ADAM 33
- PDB DOI: https://doi.org/10.2210/pdb1R55/pdb
- Classification: HYDROLASE
- Organism(s): Homo sapiens
- Expression System: Drosophila melanogaster
- Mutation(s): Yes 
- Deposited: 2003-10-09 Released: 2004-10-12 
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.58 Å
- R-Value Free: 0.219 
- R-Value Work: 0.207 
- R-Value Observed: 0.210 
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 |
ADAM 33 | 214 | Homo sapiens | Mutation(s): 1  Gene Names: ADAM33 EC: 3.4.24 | ||
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for Q9BZ11 (Homo sapiens) Explore Q9BZ11  Go to UniProtKB:  Q9BZ11 | |||||
PHAROS:  Q9BZ11 GTEx:  ENSG00000149451  | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | Q9BZ11 | ||||
Sequence AnnotationsExpand | |||||
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Oligosaccharides
Entity ID: 2 | |||||
---|---|---|---|---|---|
Molecule | Chains | Length | 2D Diagram | Glycosylation | 3D Interactions |
alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | B | 5 | N-Glycosylation | ||
Glycosylation Resources | |||||
GlyTouCan:  G21381MC GlyCosmos:  G21381MC GlyGen:  G21381MC |
Small Molecules
Ligands 4 Unique | |||||
---|---|---|---|---|---|
ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
097 Query on 097 | G [auth A] | (2S,3R)-N~4~-[(1S)-2,2-dimethyl-1-(methylcarbamoyl)propyl]-N~1~,2-dihydroxy-3-(2-methylpropyl)butanediamide C15 H29 N3 O5 OCSMOTCMPXTDND-OUAUKWLOSA-N | |||
ZN Query on ZN | C [auth A] | ZINC ION Zn PTFCDOFLOPIGGS-UHFFFAOYSA-N | |||
CA Query on CA | D [auth A] | CALCIUM ION Ca BHPQYMZQTOCNFJ-UHFFFAOYSA-N | |||
CL Query on CL | E [auth A], F [auth A] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.58 Å
- R-Value Free: 0.219 
- R-Value Work: 0.207 
- R-Value Observed: 0.210 
- Space Group: C 2 2 21
Unit Cell:
Length ( Å ) | Angle ( ˚ ) |
---|---|
a = 57.99 | α = 90 |
b = 65.205 | β = 90 |
c = 99.679 | γ = 90 |
Software Name | Purpose |
---|---|
MAR345 | data collection |
SCALEPACK | data scaling |
AMoRE | phasing |
CNS | refinement |
Entry History 
Deposition Data
- Released Date: 2004-10-12  Deposition Author(s): Orth, P., Reichert, P., Wang, W., Prosise, W.W., Yarosh-Tomaine, T., Hammond, G., Xiao, L., Mirza, U.A., Zou, J., Strickland, C., Taremi, S.S., Le, H.V., Madison, V.
Revision History (Full details and data files)
- Version 1.0: 2004-10-12
Type: Initial release - Version 1.1: 2008-04-29
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Non-polymer description, Version format compliance - Version 1.3: 2017-10-11
Changes: Refinement description - Version 2.0: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Advisory, Atomic model, Data collection, Database references, Derived calculations, Structure summary - Version 2.1: 2021-10-27
Changes: Database references, Structure summary