1cge

CRYSTAL STRUCTURES OF RECOMBINANT 19-KDA HUMAN FIBROBLAST COLLAGENASE COMPLEXED TO ITSELF

Method: X-RAY DIFFRACTION Dmax: 54.3 Å Quality: REASONABLE

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

FIBROBLAST COLLAGENASE

Homo sapiens

UniProt P03956

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 102–269 Not recorded ZN ZINC ION × 2 CA CALCIUM ION × 3 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.90 Å

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.

13 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MMP1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–168; UniProt 102–269

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 1cge

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1cge
Deposition date deposition_date1994-02-03
Structure title titleCRYSTAL STRUCTURES OF RECOMBINANT 19-KDA HUMAN FIBROBLAST COLLAGENASE COMPLEXED TO ITSELF
Keywords keywordsHYDROLASE (METALLOPROTEASE); HYDROLASE (METALLOPROTEASE)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.19
Radius of gyration Rg (electron density) rg_electron14.95
Forward intensity I(0) i06948510.00
Molecular weight molecular_weight18141.0 kDa
Excluded volume excluded_volume22168 ų
Envelope volume envelope_volume25002 ų
Hydration-shell volume shell_volume14042 ų
Envelope diameter envelope_diameter55.5
Shell Rg shell_rg21.02
Envelope Rg envelope_rg15.35
Shape Rg shape_rg14.94
Total Rg total_rg16.08
Total atoms total_atoms1547
Residues n_residues162
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 dmax54.3
Rg (real space) rg_real16.08
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real6.9490e+06
I(0) uncertainty (real space) i0_real_error7.8420e+04
Rg (reciprocal space) rg_reciprocal16.09
I(0) (reciprocal space) i0_reciprocal6949000.0000
Solution quality estimate total_estimate0.6372
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary20.9
Skewness Skewness skewness0.148
Kurtosis Kurtosis kurtosis-0.253
Angular range angular_range— – 0.4900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1213000.0000
Real-space data points n_real_points79
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.742; Stabil: 1.000; Sysdev: 0.353; Positv: 1.000; Valcen: 0.995; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1cgea_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.92 — Zincin-like
Superfamily Superfamily superfamilyd.92.1 — Metalloproteases ('zincins'), catalytic domain
Family Family familyd.92.1.11 — Matrix metalloproteases, catalytic domain

CATH v4.4 (1 domains)

Domain ID domain_id1cgeA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology390 — Collagenase (Catalytic Domain)
Homologous superfamily homologous superfamily10 — Collagenase (Catalytic Domain)

8. Citations (2)

9. Files and Curves (10)