2PX9: SUMO-activating enzyme subunit 2

The intrinsic affinity between E2 and the Cys domain of E1 in Ubiquitin-like modifications. Determined by solution NMR. Released 24 Jul 2007.

Method: Solution NMR
Organism: Homo sapiens
Chains: 2
Atoms: 3,013
Mol. weight: 42.86 kDa
Released: 24 Jul 2007

Explore 2PX9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2PX9 contains 23 α-helices and 8 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 17 helices, 0 β-strands

Element	Residues	Length
α-helix	167-169	3
α-helix	172-176	5
α-helix	182-197	16
α-helix	208-209	2
α-helix	240-246	7
α-helix	251-256	6
α-helix	257-262	6
α-helix	263-266	4
α-helix	270-272	3
α-helix	277-279	3
α-helix	284-288	5
α-helix	308-310	3
α-helix	315-336	22
α-helix	342-344	3
α-helix	349-365	17
α-helix	368-370	3
α-helix	373-381	9

Chain B: 6 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	4-18	15
β-strand	25	1	1
β-strand	28-29	2	1
β-strand	37-46	10	1
α-helix	47-48	2
β-strand	57-63	7	1
β-strand	75-77	3	1
β-strand	86	1	2
β-strand	91	1	1
β-strand	92	1	2
α-helix	95-97	3
α-helix	109-121	13
α-helix	131-139	9
α-helix	141-154	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
SUMO-activating enzyme subunit 2	A	protein	217	Homo sapiens	Q9UBT2 (AlphaFold model)
SUMO-conjugating enzyme UBC9	B	protein	158	Homo sapiens	P63279 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2PX9_1 SUMO-activating enzyme subunit 2 (chains A)
TQRTFPGCTIRNTPSEPIHCIVWAKYLFNQLFGEEDADQEVSPDRADPEAAWEPTEAEAR
ARASNEDGDIKRISTKEWAKSTGYDPVKLFTKLFKDDIRYLLTMDKLWRKRKPPVPLDWA
EVQSQGEETNASDQQNEPQLGLKDQQVLDVKSYARLFSKSIETLRVHLAEKGDGAELIWD
KDDPSAMDFVTSAANLRMHIFSMNMKSRFDIKSMAGN

Sequence of entity 2 (B), FASTA

>2PX9_2 SUMO-conjugating enzyme UBC9 (chains B)
MSGIALSRLAQERKAWRKDHPFGFVAVPTKNPDGTMNLMNWECAIPGKKGTPWEGGLFKL
RMLFKDDYPSSPPKCKFEPPLFHPNVYPSGTVCLSILEEDKDWRPAITIKQILLGIQELL
NEPNIQDPAQAEAYTIYCQNRVEYEKRVRAQAKKFAPS

Primary citation

The intrinsic affinity between E2 and the Cys domain of E1 in ubiquitin-like modifications. Wang, J., Hu, W., Cai, S. et al. Mol Cell (2007) 27:228-237. DOI 10.1016/j.molcel.2007.05.023 · PubMed

Other PDB entries of the same protein (UniProt Q9UBT2 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9QN5 1.97 Å, Crystal structure of human SUMO E1 with small unit cell parameters in the P1 21 1 space…
6XOG 1.98 Å, Structure of SUMO1-ML786519 adduct bound to SAE
6XOI 2.0 Å, Structure of SUMO1-ML00752641 adduct bound to SAE
5FQ2 2.2 Å, Crystal structure of human SUMO E1 UFD domain in complex with Ubc9 in a P422 space group.
6XOH 2.23 Å, Structure of SUMO1-ML00789344 adduct bound to SAE
1Y8Q 2.25 Å, Sumo E1 activating enzyme SAE1-SAE2-MG-ATP complex
3KYC 2.45 Å, Human SUMO E1 complex with a SUMO1-AMP mimic
6CWY 2.46 Å, Crystal structure of SUMO E1 in complex with an allosteric inhibitor
4W5V 2.5 Å, Crystal structure of Human SUMO E2-conjugating enzyme (Ubc9) in complex with…
9IF6 2.51 Å, Crystal structure of human SUMO E1 with large unit cell parameters in the P1 21 1 space…
3KYD 2.61 Å, Human SUMO E1~SUMO1-AMP tetrahedral intermediate mimic
9DRJ 2.7 Å, Cryo-EM structure of a SUMO E1-E2-SUMO1 complex.

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