5SZK: Human N-terminally engineered Rab1b

Structure of human N-terminally engineered Rab1b in complex with the bMERB domain of Mical-cL. Determined by X-ray diffraction at 2.8 Å resolution. Released 24 Aug 2016.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,601
Mol. weight: 41.37 kDa
Ligands: GNP, MG
Released: 24 Aug 2016

Explore 5SZK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5SZK contains 11 α-helices and 6 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: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	538-570	33
α-helix	584-631	48
α-helix	640-677	38

Chain B: 8 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	7-15	9	1
α-helix	21-30	10
β-strand	43-52	10	1
β-strand	55-64	10	1
α-helix	68-70	3
α-helix	71-75	5
α-helix	76-78	3
β-strand	83-89	7	1
α-helix	93-97	5
α-helix	99-109	11
β-strand	115-121	7	1
α-helix	133-140	8
β-strand	147-149	3	1
α-helix	158-171	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
MICAL C-terminal-like protein	A	protein	153	Homo sapiens	O94851 (AlphaFold model)
Ras-related protein Rab-1B	B	protein	203	Homo sapiens	Q9H0U4 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5SZK_1 MICAL C-terminal-like protein (chains A)
GHMKQEELKRLYKAQAIQRQLEEVEERQRASEIQGVRLEKALRGEADSGTQDEAQLLQEW
FKLVLEKNKLMRYESELLIMAQELELEDHQSRLEQKLREKMLKEESQKDEKDLNEEQEVF
TELMQVIEQRDKLVDSLEEQRIREKAEDQHFES

Sequence of entity 2 (B), FASTA

>5SZK_2 Ras-related protein Rab-1B (chains B)
GHMAKTYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIK
LQIWDTAGQERFRTITSSYYRGAHGIIVVYDVTDQESYANVKQWLQEIDRYASENVNKLL
VGNKSDLTTKKVVDNTTAKEFADSLGIPFLETSAKNATNVEQAFMTMAAEIKKRMGPGAA
SGGERPNLKIDSTPVKPAGGGCC

Ligands and cofactors

ID	Name	Formula	Copies
GNP	Phosphoaminophosphonic acid-guanylate ester	C10 H17 N6 O13 P3	1
MG	Magnesium ion	Mg	1

Primary citation

bMERB domains are bivalent Rab8 family effectors evolved by gene duplication. Rai, A., Oprisko, A., Campos, J. et al. Elife (2016) 5. DOI 10.7554/eLife.18675 · PubMed

Other PDB entries of the same protein (UniProt O94851 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5SZH 2.3 Å, Structure of human Rab1b in complex with the bMERB domain of Mical-cL
5SZJ 2.66 Å, Structure of human Rab10 in complex with the bMERB domain of Mical-cL
5SZI 2.85 Å, Structure of human Rab8a in complex with the bMERB domain of Mical-cL
2E9K Solution structure of the CH domain from human MICAL-2

Browse structure collections

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