6qed

CRYSTAL STRUCTURE OF HUMAN METHIONINE AMINOPEPTIDASE-2 IN COMPLEX; WITH AN INHIBITOR (S)-3-Hydroxy-2-oxo-1-(2-oxo-1,2,3,4-tetrahydro-quinolin-6-yl)-pyrrolidine-3-carboxylic acid 3-chloro-5-fluoro-benzylamide

Method: X-RAY DIFFRACTION Dmax: 68.2 Å Quality: REASONABLE

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

Methionine aminopeptidase 2

Homo sapiens

UniProt P50579

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 108–478 Not recorded EDO 1,2-ETHANEDIOL × 3 DMS DIMETHYL SULFOXIDE × 1 GOL GLYCEROL × 1 HZK (3~{S})-~{N}-[(3-chloranyl-5-fluoranyl-phenyl)methyl]-3-oxidanyl-2-oxidanylidene-1-(2-oxidanylidene-3,4-dihydro-1~{H}-quinolin-6-yl)pyrrolidine-3-carboxamide × 1 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;277 K;20% METHANOL, 0.1 M CITRATE, PH 6.0 Resolution 1.80 Å R-free 0.198

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.

39 other PDB entries and 39 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MAP2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–372; UniProt 108–478

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 6qed

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6qed
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6qed
Deposition date deposition_date2019-01-07
Structure title titleCRYSTAL STRUCTURE OF HUMAN METHIONINE AMINOPEPTIDASE-2 IN COMPLEX; WITH AN INHIBITOR (S)-3-Hydroxy-2-oxo-1-(2-oxo-1,2,3,4-tetrahydro-quinolin-6-yl)-pyrrolidine-3-carboxylic acid 3-chloro-5-fluoro-benzylamide
Keywords keywordsHYDROLASE, PEPTIDASE, METAL ION BINDING, PROTEOLYSIS, HYDROLASE-HYDROLASE INHIBITOR COMPLEX; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.47
Radius of gyration Rg (electron density) rg_electron20.52
Forward intensity I(0) i030706500.00
Molecular weight molecular_weight41655.0 kDa
Excluded volume excluded_volume51732 ų
Envelope volume envelope_volume59896 ų
Hydration-shell volume shell_volume23806 ų
Envelope diameter envelope_diameter71.5
Shell Rg shell_rg27.79
Envelope Rg envelope_rg21.13
Shape Rg shape_rg20.52
Total Rg total_rg21.41
Total atoms total_atoms2910
Residues n_residues365
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 dmax68.2
Rg (real space) rg_real21.36
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real3.0710e+07
I(0) uncertainty (real space) i0_real_error3.7770e+05
Rg (reciprocal space) rg_reciprocal21.38
I(0) (reciprocal space) i0_reciprocal30710000.0000
Solution quality estimate total_estimate0.6536
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.1
Skewness Skewness skewness0.204
Kurtosis Kurtosis kurtosis-0.430
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11800000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.884; Stabil: 0.999; Sysdev: 0.281; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id6qedA01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology230 — Creatine Amidinohydrolase
Homologous superfamily homologous superfamily10 — Creatinase/methionine aminopeptidase superfamily
Domain ID domain_id6qedA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily10 — Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain

8. Citations (1)

9. Files and Curves (10)