1ABF

SUBSTRATE SPECIFICITY AND AFFINITY OF A PROTEIN MODULATED BY BOUND WATER MOLECULES

PDB DOI: https://doi.org/10.2210/pdb1ABF/pdb

Classification: BINDING PROTEIN
Organism(s): Escherichia coli
Mutation(s): No

Deposited: 1992-04-23 Released: 1993-10-31
Deposition Author(s): Wilson, D.K., Quiocho, F.A.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.90 Å
R-Value Observed: 0.134

wwPDB Validation 3D Report Full Report

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

Macromolecule Content

Total Structure Weight: 33.58 kDa
Atom Count: 2,528
Modelled Residue Count: 305
Deposited Residue Count: 306
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
L-ARABINOSE-BINDING PROTEIN	A	306	Escherichia coli	Mutation(s): 0
UniProt
Find proteins for P02924 (Escherichia coli (strain K12)) Explore P02924 Go to UniProtKB: P02924
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P02924
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 2 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
FCB Query on FCB Download Ideal Coordinates CCD File SDF format, chain C [auth A] MOL2 format, chain C [auth A]	C [auth A]	beta-D-fucopyranose C₆ H₁₂ O₅ SHZGCJCMOBCMKK-FPRJBGLDSA-N		Interactions Focus chain C [auth A]
FCA Query on FCA Download Ideal Coordinates CCD File SDF format, chain B [auth A] MOL2 format, chain B [auth A]	B [auth A]	alpha-D-fucopyranose C₆ H₁₂ O₅ SHZGCJCMOBCMKK-PHYPRBDBSA-N		Interactions Focus chain B [auth A]

Binding Affinity Annotations
ID	Source	Binding Affinity
FCB	Binding MOAD: 1ABF	Kd: 3800 (nM) from 1 assay(s)
FCA	Binding MOAD: 1ABF	Kd: 3800 (nM) from 1 assay(s)

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.90 Å
R-Value Observed: 0.134
Space Group: P 2₁ 2₁ 2₁

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 55.92	α = 90
b = 72.02	β = 90
c = 78.02	γ = 90

Software Package:

Software Name	Purpose
PROLSQ	refinement

Structure Validation

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Entry History

Deposition Data

Released Date: 1993-10-31

Deposition Author(s):

Wilson, D.K.

Quiocho, F.A.

Revision History (Full details and data files)

Version 1.0: 1993-10-31
Type: Initial release
Version 1.1: 2008-03-10
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Data collection, Derived calculations, Other, Structure summary
Version 1.4: 2024-02-07
Changes: Data collection, Database references, Structure summary

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Deposit Data

Help and Resources

1ABF

SUBSTRATE SPECIFICITY AND AFFINITY OF A PROTEIN MODULATED BY BOUND WATER MOLECULES

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)