1MX1

Crystal Structure of Human Liver Carboxylesterase in complex with tacrine

PDB DOI: https://doi.org/10.2210/pdb1MX1/pdb

Classification: HYDROLASE
Organism(s): Homo sapiens
Expression System: Spodoptera frugiperda
Mutation(s): No

Deposited: 2002-10-01 Released: 2003-04-22
Deposition Author(s): Bencharit, S., Morton, C.L., Hyatt, J.L., Kuhn, P., Danks, M.K., Potter, P.M., Redinbo, M.R.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.40 Å
R-Value Free: 0.207
R-Value Work: 0.162
R-Value Observed: 0.162

wwPDB Validation 3D Report Full Report

This is version 2.0 of the entry. See complete history.

Macromolecule Content

Total Structure Weight: 367.25 kDa
Atom Count: 27,468
Modelled Residue Count: 3,187
Deposited Residue Count: 3,288
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
liver Carboxylesterase I	A, B, C, D, E A, B, C, D, E, F	548	Homo sapiens	Mutation(s): 0 EC: 3.1.1.1
UniProt & NIH Common Fund Data Resources
Find proteins for P23141 (Homo sapiens) Explore P23141 Go to UniProtKB: P23141
PHAROS: P23141 GTEx: ENSG00000198848
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P23141
Sequence Annotations Expand
Reference Sequence

Oligosaccharides

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Entity ID: 2
Molecule	Chains	Length	2D Diagram	Glycosylation	3D Interactions
2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose	G	2		N-Glycosylation	Interactions Focus chain G
Glycosylation Resources
GlyTouCan: G07375KG GlyCosmos: G07375KG GlyGen: G07375KG

Small Molecules

Ligands 3 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
SIA Query on SIA Download Ideal Coordinates CCD File SDF format, chain I [auth A] SDF format, chain P [auth D] SDF format, chain L [auth B] SDF format, chain S [auth E] MOL2 format, chain I [auth A] MOL2 format, chain P [auth D] MOL2 format, chain L [auth B] MOL2 format, chain S [auth E]	I [auth A], L [auth B], P [auth D], S [auth E]	N-acetyl-alpha-neuraminic acid C₁₁ H₁₉ N O₉ SQVRNKJHWKZAKO-YRMXFSIDSA-N		Interactions Focus chain I [auth A] Focus chain L [auth B] Focus chain P [auth D] Focus chain S [auth E]
NAG Query on NAG Download Ideal Coordinates CCD File SDF format, chain K [auth B] SDF format, chain R [auth E] SDF format, chain U [auth F] SDF format, chain V [auth F] SDF format, chain H [auth A] SDF format, chain O [auth D] MOL2 format, chain K [auth B] MOL2 format, chain R [auth E] MOL2 format, chain U [auth F] MOL2 format, chain V [auth F] MOL2 format, chain H [auth A] MOL2 format, chain O [auth D]	H [auth A] K [auth B] O [auth D] R [auth E] U [auth F] H [auth A], K [auth B], O [auth D], R [auth E], U [auth F], V [auth F]	2-acetamido-2-deoxy-beta-D-glucopyranose C₈ H₁₅ N O₆ OVRNDRQMDRJTHS-FMDGEEDCSA-N		Interactions Focus chain H [auth A] Focus chain K [auth B] Focus chain O [auth D] Focus chain R [auth E] Focus chain U [auth F] Focus chain V [auth F]
THA Query on THA Download Ideal Coordinates CCD File SDF format, chain Q [auth D] SDF format, chain W [auth F] SDF format, chain J [auth A] SDF format, chain M [auth B] SDF format, chain N [auth C] SDF format, chain T [auth E] MOL2 format, chain Q [auth D] MOL2 format, chain W [auth F] MOL2 format, chain J [auth A] MOL2 format, chain M [auth B] MOL2 format, chain N [auth C] MOL2 format, chain T [auth E]	J [auth A] M [auth B] N [auth C] Q [auth D] T [auth E] J [auth A], M [auth B], N [auth C], Q [auth D], T [auth E], W [auth F]	TACRINE C₁₃ H₁₄ N₂ YLJREFDVOIBQDA-UHFFFAOYSA-N		Interactions Focus chain J [auth A] Focus chain M [auth B] Focus chain N [auth C] Focus chain Q [auth D] Focus chain T [auth E] Focus chain W [auth F]

Binding Affinity Annotations
ID	Source	Binding Affinity
THA	BindingDB: 1MX1	Ki: 1.00e+5 (nM) from 1 assay(s)
	BindingDB: 1MX1	IC50: 1.00e+5 (nM) from 1 assay(s)
	PDBBind: 1MX1	Ki: 1.00e+5 (nM) from 1 assay(s)

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.40 Å
R-Value Free: 0.207
R-Value Work: 0.162
R-Value Observed: 0.162
Space Group: P 1 2₁ 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 90.021	α = 90
b = 117.03	β = 95.69
c = 176.01	γ = 90

Software Package:

Software Name	Purpose
MOSFLM	data reduction
SCALEPACK	data scaling
AMoRE	phasing
CNS	refinement

Structure Validation

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Entry History

Deposition Data

Released Date: 2003-04-22

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2003-04-22
Type: Initial release
Version 1.1: 2008-04-28
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Non-polymer description, Version format compliance
Version 2.0: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Advisory, Atomic model, Data collection, Database references, Derived calculations, Structure summary

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Deposit Data

Help and Resources

1MX1

Crystal Structure of Human Liver Carboxylesterase in complex with tacrine

Entity ID: 1

UniProt & NIH Common Fund Data Resources

Entity Groups

Sequence Annotations

Expand

Entity ID: 2

Glycosylation Resources

Experimental Data

Structure Validation

Deposition Data

Revision History (Full details and data files)