1HUR: Human ADP-ribosylation factor 1

Human ADP-ribosylation factor 1 complexed with GDP, full length non-myristoylated. Determined by X-ray diffraction at 2.0 Å resolution. Released 10 Jul 1995.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,045
Mol. weight: 42.12 kDa
Ligands: MG, GDP
Released: 10 Jul 1995

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

Secondary structure: helices and β-sheets

1HUR contains 19 α-helices and 18 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: 9 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	6-9	4
β-strand	19-24	6	1
α-helix	30-36	7
β-strand	42-45	4	1
β-strand	53-58	6	1
β-strand	61-67	7	1
α-helix	79-82	4
β-strand	85-93	9	1
α-helix	100-111	12
α-helix	114-116	3
β-strand	120-126	7	1
α-helix	133-135	3
α-helix	136-143	8
α-helix	145-147	3
β-strand	153-157	5	1
β-strand	159	1	2
β-strand	164	1	2
α-helix	166-179	14

Chain B: 10 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	4-8	5
β-strand	18-24	7	1
α-helix	30-37	8
β-strand	42-48	7	1
β-strand	51-58	8	1
β-strand	61-67	7	1
α-helix	76-81	6
α-helix	82-84	3
β-strand	85-93	9	1
α-helix	97-99	3
α-helix	100-111	12
α-helix	119	1
β-strand	120-126	7	1
α-helix	133-135	3
α-helix	136-143	8
β-strand	153-157	5	1
β-strand	159	1	3
β-strand	164	1	3
α-helix	166-176	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Human ADP-ribosylation factor 1	A, B	protein	180	Homo sapiens	P84077 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1HUR_1 HUMAN ADP-RIBOSYLATION FACTOR 1 (chains A, B)
GNIFANLFKGLFGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNI
SFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVL
LVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLSNQLRNQK

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	2
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	2

Primary citation

Structure of the human ADP-ribosylation factor 1 complexed with GDP. Amor, J.C., Harrison, D.H., Kahn, R.A. et al. Nature (1994) 372:704-708. DOI 10.1038/372704a0 · PubMed

Other PDB entries of the same protein (UniProt P84077 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8SDW 1.75 Å, Crystal structure of the non-myristoylated mutant [L8K]Arf1 in complex with a GDP analogue
7R4H 2.34 Å, phospho-STING binding to adaptor protein complex-1
6FAE 2.35 Å, The Sec7 domain of IQSEC2 (Brag1) in complex with the small GTPase Arf1
1RE0 2.4 Å, Structure of ARF1-GDP bound to Sec7 domain complexed with Brefeldin A
9QLO 2.47 Å, NMT1-NAC bound human RNC with full length ARF1 - State 1
9QLQ 2.57 Å, NMT1-NAC bound human RNC with full length ARF1 - alternative State
7DN8 2.61 Å, Crystal structure of Salmonella effector SopF in complex with ARF1
9QLP 2.75 Å, NMT1-NAC bound human RNC with full length ARF1 - State 2
3O47 2.8 Å, Crystal structure of ARFGAP1-ARF1 fusion protein
7DN9 3.29 Å, Crystal structure of Salmonella effector in complex with NAD and host co-factor ARF1
6CM9 3.73 Å, Structure of the cargo bound AP-1:Arf1:tetherin-Nef closed trimer monomeric subunit
6DFF 3.9 Å, Structure of the cargo bound AP-1:Arf1:tetherin-Nef monomer

Browse structure collections

About this viewer

MolViewer shows 1HUR directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.