1ZGU: Human Mms2-Ubiquitin complex

Solution structure of the human Mms2-Ubiquitin complex. Determined by solution NMR. Released 4 Apr 2006.

Method: Solution NMR
Organism: Homo sapiens
Chains: 2
Atoms: 1,712
Mol. weight: 24.44 kDa
Released: 4 Apr 2006

Explore 1ZGU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1ZGU contains 11 α-helices and 16 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: 8 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	14-29	16
β-strand	36-40	5	1
β-strand	51-56	6	1
α-helix	57-58	2
β-strand	67-73	7	1
α-helix	82-83	2
β-strand	84-87	4	1
β-strand	89	1	2
β-strand	96	1	3
β-strand	102	1	1
β-strand	103	1	3
α-helix	104	1
α-helix	109-112	4
α-helix	120-131	12
α-helix	134-137	4
α-helix	140-142	3
β-strand	147	1	2

Chain B: 3 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	2-7	6	4
β-strand	12-16	5	4
β-strand	22	1	5
α-helix	23-33	11
α-helix	38-40	3
β-strand	41-45	5	4
β-strand	48-49	2	4
β-strand	55	1	5
α-helix	56-59	4
β-strand	66-71	6	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin-conjugating enzyme E2 variant 2	A	protein	139	Homo sapiens	Q15819 (AlphaFold model)
Ubiquitin	B	protein	76	Homo sapiens	P0CG48 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1ZGU_1 Ubiquitin-conjugating enzyme E2 variant 2 (chains A)
VKVPRNFRLLEELEEGQKGVGDGTVSWGLEDDEDMTLTRWTGMIIGPPRTNYENRIYSLK
VECGPKYPEAPPSVRFVTKINMNGINNSSGMVDARSIPVLAKWQNSYSIKVVLQELRRLM
MSKENMKLPQPPEGQTYNN

Sequence of entity 2 (B), FASTA

>1ZGU_2 Ubiquitin (chains B)
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGRQLEDGRTLSDYN
IQKESTLHLVLRLRGG

Primary citation

Structural Basis for Non-Covalent Interaction Between Ubiquitin and the Ubiquitin Conjugating Enzyme Variant Human MMS2. Lewis, M.J., Saltibus, L.F., Hau, D.D. et al. J Biomol NMR (2006) 34:89-100. DOI 10.1007/s10858-005-5583-6 · PubMed

Other PDB entries of the same protein (UniProt Q15819 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4ONL 1.35 Å, Crystal structure of human Mms2/Ubc13_D81N, R85S, A122V, N123P
4ONM 1.35 Å, Crystal structure of human Mms2/Ubc13 - NSC697923
4ONN 1.5 Å, Crystal structure of human Mms2/Ubc13 - BAY 11-7082
9BIV 1.68 Å, Crystal Structure of Ubc13 with a New Active Site Loop Conformation
9LHJ 1.68 Å, UBE2N/UBE2V2 complexed with a covalent inhibitor
8WR5 1.7 Å, The Crystal Structure of Mms2 from Biortus
4NR3 1.8 Å, Crystal Structure of a human Mms2/Ubc13 L121G mutant
1J7D 1.85 Å, Crystal Structure of hMms2-hUbc13
1J74 1.9 Å, Crystal Structure of Mms2
4NRG 1.95 Å, Crystal Structure of a human Mms2/Ubc13 D118G mutant
9N1F 2.1 Å, Crystal Structure of the Ark2C-Ubc13~Ub-Mms2 complex
7BBD 2.2 Å, Crystal structure of monoubiquitinated TRIM21 RING (Ub-RING) In complex with ubiquitin…

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