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2lnl

Structure of human CXCR1 in phospholipid bilayers

Method: SOLID-STATE NMR Dmax: 65.3 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

C-X-C chemokine receptor type 1

Homo sapiens

UniProt P25024

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 20–328 Fragment：UNP residues 20-328 No other associated polymer SOLID-STATE NMR NMR measurement conditions：pH 7；298 K；Ionic strength (raw mmCIF value) 20；Pressure ambient NMR sample composition：2-4 mg [U-100% 13C; U-100% 15N] CXCR1, 100% H2O | 100% H2O Resolution not provided

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 2LNL Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1ILP CXCR-1 N-TERMINAL PEPTIDE BOUND TO INTERLEUKIN-8 Deposited 1998-12-16 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain C 9–29（21 aa） Fragment：9-29
Mutation：L15 - G19 REPLACED BY 5-AMINOVALERIC ACID Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.5；308 K；Ionic strength (raw mmCIF value) 0.15 M；Pressure 1
Resolution not provided
1ILQ CXCR-1 N-TERMINAL PEPTIDE BOUND TO INTERLEUKIN-8 (MINIMIZED MEAN) Deposited 1998-12-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain C 20–29（10 aa） Fragment：9-29
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.5；308 K；Ionic strength (raw mmCIF value) 0.15 M；Pressure 1
Resolution not provided
6XMN Solution NMR CXCL8-CXCR1 N-domain complex structure Deposited 2020-06-30 Different construct Different oligomeric state Different experimental method Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–29（29 aa） Fragment：N-terminal residues 1-29
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6；303 K；Ionic strength (raw mmCIF value) 50；Pressure 1
NMR sample composition 0.4 mM [U-13C; U-15N] CXCL8, 1.2 mM CXCR1, 50 mM sodium phosphate, 0.01 % sodium azide, 10 % [U-100% 2H] D2O, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1.2 mM CXCL8, 0.5 mM [U-13C; U-15N] CXCR1, 50 mM sodium phosphate, 0.01 % sodium azide, 10 % [U-100% 2H] D2O, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
8IC0 Cryo-EM structure of CXCL8 bound C-X-C chemokine receptor 1 in complex with Gi heterotrimer Deposited 2023-02-10 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain A 1–350（350 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5；50 mM HEPES pH8.0, 100 mM NaCl, 1 mM MgCl2, 0.5 mM TCEP, 0.001% LMNG, 0.0001% CHS, 1 uM IL8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.41 Å

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CXCR1_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–309； UniProt 20–328

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 2lnl

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2lnl
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2lnl
Deposition date deposition_date2011-12-31
Structure title titleStructure of human CXCR1 in phospholipid bilayers
Keywords keywordsG protein coupled receptor, GPCR, chemokine, membrane protein, transmembrane, 7TM, phospholipid, signaling, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodSOLID-STATE NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier21.04 Å
Radius of gyration Rg (electron density) rg_electron20.81 Å
Forward intensity I(0) i01277870000.00
Molecular weight molecular_weight336880.0 kDa
Excluded volume excluded_volume435620 ų
Envelope volume envelope_volume70551 ų
Hydration-shell volume shell_volume26190 ų
Envelope diameter envelope_diameter72.0 Å
Shell Rg shell_rg29.79 Å
Envelope Rg envelope_rg22.66 Å
Shape Rg shape_rg20.80 Å
Total Rg total_rg21.03 Å
Total atoms total_atoms48570
Residues n_residues2960
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax65.3 Å
Rg (real space) rg_real21.04 Å
Rg uncertainty (real space) rg_real_error0.34 Å
I(0) (real space) i0_real1.2780e+09
I(0) uncertainty (real space) i0_real_error1.6390e+07
Rg (reciprocal space) rg_reciprocal21.05 Å
I(0) (reciprocal space) i0_reciprocal1278000000.0000
Solution quality estimate total_estimate0.9054
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.6 Å
Skewness Skewness skewness0.307
Kurtosis Kurtosis kurtosis-0.503
Angular range angular_range— – 0.3800 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1521000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.934; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.970
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2lnlA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1070 — Rhopdopsin 7-helix transmembrane proteins
Homologous superfamily homologous superfamily10 — Rhodopsin 7-helix transmembrane proteins
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8. Citations (1)

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9. Files and Curves (10)