1cl7

ANTI HIV1 PROTEASE FAB

Method: X-RAY DIFFRACTION Dmax: 79.8 Å Quality: EXCELLENT

1. Protein Identity and Related Structures Protein Identity & Related Structures

PROTEIN (IGG1 ANTIBODY 1696 (constant heavy chain))

OrganismNot specified

UniProt P01869

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain I; UniProt 133–214 Fragment:FAB PROTEIN (IGG1 ANTIBODY 1696 (light chain)) × 1 PROTEIN (IGG1 ANTIBODY 1696 (variable heavy chain)) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;pH 7.0 Resolution 3.00 Å R-free 0.280

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.

14 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGH1M_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain I; PDBConstruct 1–82; UniProt 133–214

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 1cl7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1cl7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1cl7
Deposition date deposition_date1999-05-06
Structure title titleANTI HIV1 PROTEASE FAB
Keywords keywordsFAB FRAGMENT, CROSS-REACTIVITY, HIV1 PROTEASE, ENZYME INHIBITION, IMMUNOGLOBULIN, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier25.97
Radius of gyration Rg (electron density) rg_electron24.82
Forward intensity I(0) i038486600.00
Molecular weight molecular_weight47612.0 kDa
Excluded volume excluded_volume59280 ų
Envelope volume envelope_volume72893 ų
Hydration-shell volume shell_volume24647 ų
Envelope diameter envelope_diameter81.9
Shell Rg shell_rg31.99
Envelope Rg envelope_rg24.48
Shape Rg shape_rg24.79
Total Rg total_rg25.69
Total atoms total_atoms3355
Residues n_residues433
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax79.8
Rg (real space) rg_real25.95
Rg uncertainty (real space) rg_real_error0.52
I(0) (real space) i0_real3.8490e+07
I(0) uncertainty (real space) i0_real_error5.4440e+05
Rg (reciprocal space) rg_reciprocal25.96
I(0) (reciprocal space) i0_reciprocal38490000.0000
Solution quality estimate total_estimate0.9142
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.8
Skewness Skewness skewness0.245
Kurtosis Kurtosis kurtosis-0.592
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6477000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.977; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.961

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1cl7.1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)
Domain ID domain_idd1cl7h1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)
Domain ID domain_idd1cl7l1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)
Domain ID domain_idd1cl7l2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)

CATH v4.4 (4 domains)

Domain ID domain_id1cl7H00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1cl7I00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1cl7L01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1cl7L02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)