3qbj

Crystal structure of dipeptidyl peptidase IV in complex with inhibitor

Method: X-RAY DIFFRACTION Dmax: 129.0 Å Quality: GOOD

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

Dipeptidyl peptidase 4

Homo sapiens

UniProt P27487

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Homooligomer Protein × 2 其他Polymer 3 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 31–766 Chain B; UniProt 31–766 Mutation:N150A, N520A 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ;alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 NXZ 1-[(3S,4S)-4-amino-1-(6-phenylpyrimidin-4-yl)pyrrolidin-3-yl]piperidin-2-one × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.21 Å R-free 0.235

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.

113 other PDB entries and 169 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPP4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–736; UniProt 31–766 Author chain B; PDBConstruct 1–736; UniProt 31–766

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 3qbj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3qbj
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3qbj
Deposition date deposition_date2011-01-13
Structure title titleCrystal structure of dipeptidyl peptidase IV in complex with inhibitor
Keywords keywords;Diabetes Mellitus, Dipeptidyl-Peptidase IV Inhibitor, Hypoglycemic Agent, Pyrrolidines, Sprague-Dawley, Structure-Activity Relationship, hydrolase, glycosylation, hydrolase-hydrolase inhibitor complex ;; hydrolase/hydrolase inhibitor
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier39.41
Radius of gyration Rg (electron density) rg_electron39.05
Forward intensity I(0) i0429141000.00
Molecular weight molecular_weight171350.0 kDa
Excluded volume excluded_volume214660 ų
Envelope volume envelope_volume284000 ų
Hydration-shell volume shell_volume59657 ų
Envelope diameter envelope_diameter133.4
Shell Rg shell_rg45.67
Envelope Rg envelope_rg38.82
Shape Rg shape_rg39.01
Total Rg total_rg39.58
Total atoms total_atoms12112
Residues n_residues1456
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 dmax129.0
Rg (real space) rg_real39.45
Rg uncertainty (real space) rg_real_error1.00
I(0) (real space) i0_real4.2910e+08
I(0) uncertainty (real space) i0_real_error6.7490e+06
Rg (reciprocal space) rg_reciprocal39.43
I(0) (reciprocal space) i0_reciprocal429100000.0000
Solution quality estimate total_estimate0.8807
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary41.9
Skewness Skewness skewness0.352
Kurtosis Kurtosis kurtosis-0.511
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha53880000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.855; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.885

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd3qbja1
Class classb — All beta proteins
Fold Fold foldb.70 — 8-bladed beta-propeller
Superfamily Superfamily superfamilyb.70.3 — DPP6 N-terminal domain-like
Family Family familyb.70.3.1 — DPP6 N-terminal domain-like
Domain ID domain_idd3qbja2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.69 — alpha/beta-Hydrolases
Superfamily Superfamily superfamilyc.69.1 — alpha/beta-Hydrolases
Family Family familyc.69.1.24 — DPP6 catalytic domain-like
Domain ID domain_idd3qbjb1
Class classb — All beta proteins
Fold Fold foldb.70 — 8-bladed beta-propeller
Superfamily Superfamily superfamilyb.70.3 — DPP6 N-terminal domain-like
Family Family familyb.70.3.1 — DPP6 N-terminal domain-like
Domain ID domain_idd3qbjb2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.69 — alpha/beta-Hydrolases
Superfamily Superfamily superfamilyc.69.1 — alpha/beta-Hydrolases
Family Family familyc.69.1.24 — DPP6 catalytic domain-like

CATH v4.4 (4 domains)

Domain ID domain_id3qbjA01
Class class2 — Mainly Beta
Architecture architecture140 — 8 Propeller
Topology topology10 — Methanol Dehydrogenase; Chain A
Homologous superfamily homologous superfamily30 — Dipeptidylpeptidase IV, N-terminal domain
Domain ID domain_id3qbjA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1820 — Alpha/Beta hydrolase fold, catalytic domain
Domain ID domain_id3qbjB01
Class class2 — Mainly Beta
Architecture architecture140 — 8 Propeller
Topology topology10 — Methanol Dehydrogenase; Chain A
Homologous superfamily homologous superfamily30 — Dipeptidylpeptidase IV, N-terminal domain
Domain ID domain_id3qbjB02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1820 — Alpha/Beta hydrolase fold, catalytic domain

8. Citations (1)

9. Files and Curves (10)