1yw8

h-MetAP2 complexed with A751277

Method: X-RAY DIFFRACTION Dmax: 66.9 Å Quality: EXCELLENT

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 110–478 Not recorded MN MANGANESE (II) ION × 2 A75 2-[(PHENYLSULFONYL)AMINO]-5,6,7,8-TETRAHYDRONAPHTHALENE-1-CARBOXYLIC ACID × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.65 Å R-free 0.273

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 AMP2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–369; UniProt 110–478

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 1yw8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1yw8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1yw8
Deposition date deposition_date2005-02-17
Structure title titleh-MetAP2 complexed with A751277
Keywords keywordsHydrolase; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.40
Radius of gyration Rg (electron density) rg_electron20.50
Forward intensity I(0) i030621500.00
Molecular weight molecular_weight41749.0 kDa
Excluded volume excluded_volume51849 ų
Envelope volume envelope_volume58958 ų
Hydration-shell volume shell_volume23585 ų
Envelope diameter envelope_diameter68.6
Shell Rg shell_rg27.75
Envelope Rg envelope_rg20.96
Shape Rg shape_rg20.50
Total Rg total_rg21.39
Total atoms total_atoms2920
Residues n_residues369
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 dmax66.9
Rg (real space) rg_real21.28
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real3.0620e+07
I(0) uncertainty (real space) i0_real_error3.7010e+05
Rg (reciprocal space) rg_reciprocal21.31
I(0) (reciprocal space) i0_reciprocal30620000.0000
Solution quality estimate total_estimate0.9023
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.6
Skewness Skewness skewness0.188
Kurtosis Kurtosis kurtosis-0.459
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9211000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.914; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.986

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1yw8a1
Class classa — All alpha proteins
Fold Fold folda.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamilya.4.5 — 'Winged helix' DNA-binding domain
Family Family familya.4.5.25 — Methionine aminopeptidase, insert domain
Domain ID domain_idd1yw8a2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.127 — Creatinase/aminopeptidase
Superfamily Superfamily superfamilyd.127.1 — Creatinase/aminopeptidase
Family Family familyd.127.1.1 — Creatinase/aminopeptidase

CATH v4.4 (2 domains)

Domain ID domain_id1yw8A01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology230 — Creatine Amidinohydrolase
Homologous superfamily homologous superfamily10 — Creatinase/methionine aminopeptidase superfamily
Domain ID domain_id1yw8A02
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)