5HL8

1.93 Angstrom resolution crystal structure of a pullulanase-specific type II secretion system integral cytoplasmic membrane protein GspL (C-terminal fragment; residues 309-397) from Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044

PDB DOI: https://doi.org/10.2210/pdb5HL8/pdb

Classification: PROTEIN TRANSPORT
Organism(s): Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2016-01-14 Released: 2016-01-27
Deposition Author(s): Halavaty, A.S., Minasov, G., Kiryukhina, O., Grimshaw, S., Light, S., Dubrovska, I., Shuvalova, L., Kwon, K., Anderson, W.F., Center for Structural Genomics of Infectious Diseases (CSGID)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.93 Å
R-Value Free: 0.281
R-Value Work: 0.226
R-Value Observed: 0.229

wwPDB Validation 3D Report Full Report

This is version 1.0 of the entry. See complete history.

Literature

1.93 Angstrom resolution crystal structure of a pullulanase-specific type II secretion system integral cytoplasmic membrane protein GspL (C-terminal fragment; residues 309-397) from Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044

Halavaty, A.S., Minasov, G., Kiryukhina, O., Grimshaw, S., Light, S., Dubrovska, I., Shuvalova, L., Kwon, K., Anderson, W.F., Center for Structural Genomics of Infectious Diseases (CSGID)

To be published.

Macromolecule Content

Total Structure Weight: 40.77 kDa
Atom Count: 2,582
Modelled Residue Count: 309
Deposited Residue Count: 368
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Type II secretion system protein L	A, B, C, D	92	Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044	Mutation(s): 0 Gene Names: pulL, KpST82_0737
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations Expand
Reference Sequence

Small Molecules

Modified Residues 1 Unique
ID	Chains	Type	Formula	2D Diagram	Parent
MSE Query on MSE	A, B, C, D	L-PEPTIDE LINKING	C₅ H₁₁ N O₂ Se		MET

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.93 Å
R-Value Free: 0.281
R-Value Work: 0.226
R-Value Observed: 0.229
Space Group: P 2₁ 2₁ 2₁
Diffraction Data: https://doi.org/10.18430/m35hl8

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 50.375	α = 90
b = 51.284	β = 90
c = 117.021	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement
HKL-3000	data reduction
HKL-3000	data scaling
HKL-3000	phasing
Coot	model building

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2016-01-27

Deposition Author(s):

Center for Structural Genomics of Infectious Diseases (CSGID)

Revision History (Full details and data files)

Version 1.0: 2016-01-27
Type: Initial release

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.