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6syf

Human Ubc9 with covalent isopeptide ligand

Method: X-RAY DIFFRACTION
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1. Protein Identity and Related Structures Protein Identity & Related Structures

SUMO-conjugating enzyme UBC9

Homo sapiens

UniProt P63279

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 3 ACE-LEU-ARG-LEU-ARG-GLY-CYS × 1 ACE-ILE-LYS-GLN-GLU × 1 water × 3 Consistent with protein count
2 Protein heterocomplex Heteromer Protein 3 ACE-LEU-ARG-LEU-ARG-GLY-CYS × 1 ACE-ILE-LYS-GLN-GLU × 1 water × 3 Consistent with protein count
3 Protein heterocomplex Heteromer Protein 3 ACE-LEU-ARG-LEU-ARG-GLY-CYS × 1 ACE-ILE-LYS-GLN-GLU × 1 water × 2 Consistent with protein count
4 Protein heterocomplex Heteromer Protein 3 ACE-LEU-ARG-LEU-ARG-GLY-CYS × 1 ACE-ILE-LYS-GLN-GLU × 1 water × 3 Consistent with protein count

Other States of the Same Protein in the Database

Monomer
1a3s 3a4s 3a4s 5f6d 5f6e 5f6u 5f6v 5f6w 5f6x 5f6y 9glr

11 assemblies

Homodimer

None

Homotetramer

None

Other homooligomers

None

Heteromeric or nucleic-acid complex
1kps 1kps 1z5s 2grn 2gro 2grp 2grq 2grr 2o25 2o25 2pe6 2px9

29 assemblies; showing the first 12

View Construct and Data Evidence
UniProt name UBC9_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 2–158； UniProt 2–158 Author chain B； PDBConstruct 2–158； UniProt 2–158 Author chain C； PDBConstruct 2–158； UniProt 2–158 Author chain D； PDBConstruct 2–158； UniProt 2–158

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id6syf
Deposition date deposition_date2019-09-27
Structure title titleHuman Ubc9 with covalent isopeptide ligand
Keywords keywordsUbc9, isopeptide, disulfide, ubiquitin, SUMO, LIGASE; LIGASE
Experimental Method methodX-RAY DIFFRACTION
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

6syf__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

6syf__assembly_1__model_1 | I(q)

10-2 10-1 105 106 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

6syf__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg（Guinier）17.14 Å
Rg (electron density)15.92 Å
Total Rg17.04 Å
Atom count1311
Residues163
Excluded volume23498 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 6syf__assembly_1__model_1 trimeric （3） Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 6syf__assembly_2__model_1 trimeric （3） Success 4.1.3-1-20251215 (887e7ef) View Download
3 1 6syf__assembly_3__model_1 trimeric （3） Success 4.1.3-1-20251215 (887e7ef) View Download
4 1 6syf__assembly_4__model_1 trimeric （3） Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (4)

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7. Citations (1)