1H1B

Crystal structure of human neutrophil elastase complexed with an inhibitor (GW475151)

PDB DOI: https://doi.org/10.2210/pdb1H1B/pdb

Classification: HYDROLASE
Organism(s): Homo sapiens
Mutation(s): No

Deposited: 2002-07-05 Released: 2002-08-29
Deposition Author(s): Macdonald, S.J.F., Dowle, M.D., Harrison, L.A., Clarke, G.D.E., Inglis, G.G.A., Johnson, M.R., Smith, R.A., Amour, A., Fleetwood, G., Humphreys, D.C., Molloy, C.R., Dixon, M., Godward, R.E., Wonacott, A.J., Singh, O.M.P., Hodgson, S.T., Hardy, G.W.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.00 Å
R-Value Free: 0.310
R-Value Work: 0.251
R-Value Observed: 0.254

wwPDB Validation 3D Report Full Report

This is version 2.1 of the entry. See complete history.

Macromolecule Content

Total Structure Weight: 48.99 kDa
Atom Count: 3,670
Modelled Residue Count: 436
Deposited Residue Count: 436
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
LEUKOCYTE ELASTASE	A, B	218	Homo sapiens	Mutation(s): 0 EC: 3.4.21.37
UniProt & NIH Common Fund Data Resources
Find proteins for P08246 (Homo sapiens) Explore P08246 Go to UniProtKB: P08246
PHAROS: P08246 GTEx: ENSG00000197561
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P08246
Sequence Annotations Expand
Reference Sequence

Oligosaccharides

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Entity ID: 2
Molecule	Chains	Length	2D Diagram	Glycosylation	3D Interactions
alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose	C, D, E, F	2		N-Glycosylation	Interactions Focus chain C Focus chain D Focus chain E Focus chain F
Glycosylation Resources
GlyTouCan: G86851RC GlyCosmos: G86851RC GlyGen: G86851RC

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
151 Query on 151 Download Ideal Coordinates CCD File SDF format, chain G [auth A] SDF format, chain H [auth B] MOL2 format, chain G [auth A] MOL2 format, chain H [auth B]	G [auth A], H [auth B]	(2S)-3-METHYL-2-((2R,3S)-3-[(METHYLSULFONYL)AMINO]-1-{[2-(PYRROLIDIN-1-YLMETHYL)-1,3-OXAZOL-4-YL]CARBONYL}PYRROLIDIN-2-YL)BUTANOIC ACID C₁₉ H₃₀ N₄ O₆ S PWBJTGRBTWYVSH-XOKHGSTOSA-N		Interactions Focus chain G [auth A] Focus chain H [auth B]

Binding Affinity Annotations
ID	Source	Binding Affinity
151	PDBBind: 1H1B	Ki: 0.16 (nM) from 1 assay(s)

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.00 Å
R-Value Free: 0.310
R-Value Work: 0.251
R-Value Observed: 0.254
Space Group: P 4₃ 2 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 68.88	α = 90
b = 68.88	β = 90
c = 241.15	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement
DENZO	data reduction
SCALEPACK	data scaling
AMoRE	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2002-08-29

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2002-08-29
Type: Initial release
Version 1.1: 2011-09-14
Changes: Derived calculations, Non-polymer description, Other, Structure summary, Version format compliance
Version 1.2: 2019-05-08
Changes: Data collection, Derived calculations, Experimental preparation, Other
Version 2.0: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Atomic model, Data collection, Derived calculations, Structure summary
Version 2.1: 2023-12-13
Changes: Data collection, Database references, Derived calculations, Refinement description, Structure summary