1b6a

HUMAN METHIONINE AMINOPEPTIDASE 2 COMPLEXED WITH TNP-470

Method: X-RAY DIFFRACTION Dmax: 67.1 Å Quality: GOOD

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

METHIONINE AMINOPEPTIDASE

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 1–478 Not recorded CO COBALT (II) ION × 2 TN4 (1R,2S,3S,4R)-4-hydroxy-2-methoxy-4-methyl-3-[(2R,3R)-2-methyl-3-(3-methylbut-2-en-1-yl)oxiran-2-yl]cyclohexyl (chloroacetyl)carbamate × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.4;pH 5.40 Resolution 1.60 Å R-free 0.216

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 AMPM2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–478; UniProt 1–478

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 1b6a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1b6a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1b6a
Deposition date deposition_date1999-01-13
Structure title titleHUMAN METHIONINE AMINOPEPTIDASE 2 COMPLEXED WITH TNP-470
Keywords keywordsANGIOGENESIS INHIBITOR, AMINOPEPTIDASE; ANGIOGENESIS INHIBITOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.00
Radius of gyration Rg (electron density) rg_electron20.05
Forward intensity I(0) i028597400.00
Molecular weight molecular_weight40285.0 kDa
Excluded volume excluded_volume50109 ų
Envelope volume envelope_volume57454 ų
Hydration-shell volume shell_volume23292 ų
Envelope diameter envelope_diameter71.4
Shell Rg shell_rg27.35
Envelope Rg envelope_rg20.69
Shape Rg shape_rg20.04
Total Rg total_rg20.99
Total atoms total_atoms2815
Residues n_residues355
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 dmax67.1
Rg (real space) rg_real20.88
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real2.8600e+07
I(0) uncertainty (real space) i0_real_error3.6720e+05
Rg (reciprocal space) rg_reciprocal20.91
I(0) (reciprocal space) i0_reciprocal28600000.0000
Solution quality estimate total_estimate0.8942
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.3
Skewness Skewness skewness0.184
Kurtosis Kurtosis kurtosis-0.432
Angular range angular_range— – 0.3800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10780000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.877; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.992

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_idd1b6aa1
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_idd1b6aa2
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_id1b6aA01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology230 — Creatine Amidinohydrolase
Homologous superfamily homologous superfamily10 — Creatinase/methionine aminopeptidase superfamily
Domain ID domain_id1b6aA02
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)