1bn5

HUMAN METHIONINE AMINOPEPTIDASE 2

Method: X-RAY DIFFRACTION Dmax: 69.2 Å Quality: REASONABLE

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 TBU TERTIARY-BUTYL ALCOHOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.4;pH 5.4 Resolution 1.80 Å R-free 0.228

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 1bn5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1bn5
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1bn5
Deposition date deposition_date1998-07-31
Structure title titleHUMAN METHIONINE AMINOPEPTIDASE 2
Keywords keywordsMETHIONINE AMINOPEPTIDASE, HYDROLASE, AMINOPEPTIDASE; AMINOPEPTIDASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.09
Radius of gyration Rg (electron density) rg_electron20.14
Forward intensity I(0) i027953900.00
Molecular weight molecular_weight39854.0 kDa
Excluded volume excluded_volume49595 ų
Envelope volume envelope_volume57585 ų
Hydration-shell volume shell_volume23298 ų
Envelope diameter envelope_diameter69.9
Shell Rg shell_rg27.43
Envelope Rg envelope_rg20.70
Shape Rg shape_rg20.14
Total Rg total_rg21.08
Total atoms total_atoms2786
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 dmax69.2
Rg (real space) rg_real20.97
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real2.7950e+07
I(0) uncertainty (real space) i0_real_error3.7780e+05
Rg (reciprocal space) rg_reciprocal20.99
I(0) (reciprocal space) i0_reciprocal27950000.0000
Solution quality estimate total_estimate0.6640
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.4
Skewness Skewness skewness0.174
Kurtosis Kurtosis kurtosis-0.444
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10420000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.841; Stabil: 1.000; Sysdev: 0.368; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

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_idd1bn5a1
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_idd1bn5a2
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_id1bn5A01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology230 — Creatine Amidinohydrolase
Homologous superfamily homologous superfamily10 — Creatinase/methionine aminopeptidase superfamily
Domain ID domain_id1bn5A02
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)