1HJK

ALKALINE PHOSPHATASE MUTANT H331Q

PDB DOI: https://doi.org/10.2210/pdb1HJK/pdb

Classification: HYDROLASE
Organism(s): Escherichia coli
Expression System: Escherichia coli
Mutation(s): Yes

Deposited: 1997-05-30 Released: 1997-10-15
Deposition Author(s): Murphy, J.E., Stec, B., Ma, L., Kantrowitz, E.R.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.30 Å
R-Value Free: 0.200
R-Value Work: 0.177
R-Value Observed: 0.177

wwPDB Validation 3D Report Full Report

This is version 1.4 of the entry. See complete history.

Literature

Trapping and visualization of a covalent enzyme-phosphate intermediate.

Murphy, J.E., Stec, B., Ma, L., Kantrowitz, E.R.

(1997) Nat Struct Biol 4: 618-622

PubMed: 9253408 Search on PubMed
DOI: https://doi.org/10.1038/nsb0897-618
Primary Citation of Related Structures:
1HJK

PubMed Abstract:
Using a mutant version of E. coli alkaline phosphatase, we succeeded in trapping and determining the structure of the phospho-enzyme intermediate. The X-ray structure also revealed the catalytic water molecule, bound to one of the active site zinc ions, positioned ideally for the apical attack necessary for the hydrolysis of the intermediate.

Macromolecule Content

Total Structure Weight: 94.83 kDa
Atom Count: 7,144
Modelled Residue Count: 898
Deposited Residue Count: 898
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
ALKALINE PHOSPHATASE	A, B	449	Escherichia coli	Mutation(s): 2 Gene Names: PHOA EC: 3.1.3.1
UniProt
Find proteins for P00634 (Escherichia coli (strain K12)) Explore P00634 Go to UniProtKB: P00634
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P00634
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 3 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
SO4 Query on SO4 Download Ideal Coordinates CCD File SDF format, chain F [auth A] SDF format, chain J [auth B] MOL2 format, chain F [auth A] MOL2 format, chain J [auth B]	F [auth A], J [auth B]	SULFATE ION O₄ S QAOWNCQODCNURD-UHFFFAOYSA-L		Interactions Focus chain F [auth A] Focus chain J [auth B]
ZN Query on ZN Download Ideal Coordinates CCD File SDF format, chain C [auth A] SDF format, chain D [auth A] SDF format, chain G [auth B] SDF format, chain H [auth B] MOL2 format, chain C [auth A] MOL2 format, chain D [auth A] MOL2 format, chain G [auth B] MOL2 format, chain H [auth B]	C [auth A], D [auth A], G [auth B], H [auth B]	ZINC ION Zn PTFCDOFLOPIGGS-UHFFFAOYSA-N		Interactions Focus chain C [auth A] Focus chain D [auth A] Focus chain G [auth B] Focus chain H [auth B]
MG Query on MG Download Ideal Coordinates CCD File SDF format, chain E [auth A] SDF format, chain I [auth B] MOL2 format, chain E [auth A] MOL2 format, chain I [auth B]	E [auth A], I [auth B]	MAGNESIUM ION Mg JLVVSXFLKOJNIY-UHFFFAOYSA-N		Interactions Focus chain E [auth A] Focus chain I [auth B]

Modified Residues 1 Unique
ID	Chains	Type	Formula	2D Diagram	Parent
SEP Query on SEP	A, B	L-PEPTIDE LINKING	C₃ H₈ N O₆ P		SER

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.30 Å
R-Value Free: 0.200
R-Value Work: 0.177
R-Value Observed: 0.177
Space Group: I 2 2 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 195.52	α = 90
b = 167.86	β = 90
c = 77.03	γ = 90

Software Package:

Software Name	Purpose
SAN	data collection
X-PLOR	model building
X-PLOR	refinement
SDMS	data reduction
X-PLOR	phasing

Structure Validation

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Entry History

Deposition Data

Released Date: 1997-10-15

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 1997-10-15
Type: Initial release
Version 1.1: 2008-03-24
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2011-11-16
Changes: Atomic model
Version 1.4: 2021-11-03
Changes: Database references, Derived calculations, Other

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1HJK

ALKALINE PHOSPHATASE MUTANT H331Q

Trapping and visualization of a covalent enzyme-phosphate intermediate.

Entity ID: 1

UniProt

Entity Groups

Sequence Annotations

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Experimental Data

Structure Validation

Deposition Data

Revision History (Full details and data files)