5WRJ: Human tyrosylprotein sulfotransferase-1

Name: PDB 5WRJ: Crystal structure of human tyrosylprotein sulfotransferase-1 complexed with PAP and gastrin peptide
Published: 2017-09-06
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transferase

Crystal structure of human tyrosylprotein sulfotransferase-1 complexed with PAP and gastrin peptide. Determined by X-ray diffraction at 2.31 Å resolution. Released 6 Sept 2017.

Method: X-ray diffraction
Resolution: 2.31 Å
Organisms: Homo sapiens, synthetic construct
Chains: 8
Atoms: 9,331
Mol. weight: 145.44 kDa
Ligands: A3P, MG
Released: 6 Sept 2017

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

Secondary structure: helices and β-sheets

5WRJ contains 66 α-helices and 33 β-strands across 5 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, 8 β-strands

Element	Residues	Length	Sheet
β-strand	72-76	5	1
α-helix	82-90	9
β-strand	95-96	2	2
α-helix	103-116	14
α-helix	118-126	9
α-helix	131-148	18
β-strand	155-156	2	2
β-strand	157-159	3	1
α-helix	161-166	6
α-helix	167-173	7
β-strand	178-183	6	1
α-helix	186-195	10
α-helix	208-229	22
β-strand	234-238	5	1
α-helix	239-244	6
α-helix	246-257	12
α-helix	263-266	4
α-helix	268-270	3
β-strand	272	1	3
β-strand	278	1	3
α-helix	287-290	4
α-helix	293-294	2
α-helix	308-312	5
α-helix	314-317	4
α-helix	320-323	4

Chain B: 16 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	72-76	5	4
α-helix	82-90	9
β-strand	95-96	2	5
α-helix	103-116	14
α-helix	118-126	9
α-helix	131-148	18
β-strand	155-156	2	5
β-strand	157-159	3	4
α-helix	161-166	6
α-helix	167-173	7
β-strand	178-183	6	4
α-helix	186-195	10
α-helix	208-229	22
β-strand	234-238	5	4
α-helix	239-244	6
α-helix	246-257	12
α-helix	263-271	9
β-strand	272	1	6
β-strand	278	1	6
α-helix	287-290	4
α-helix	293-294	2
α-helix	308-312	5
α-helix	314-317	4
α-helix	320-323	4

Chain C: 16 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	72-75	4	7
α-helix	82-90	9
β-strand	95-96	2	8
α-helix	103-116	14
α-helix	118-126	9
α-helix	131-148	18
β-strand	155-156	2	8
β-strand	157-159	3	7
α-helix	161-166	6
α-helix	167-173	7
β-strand	178-183	6	7
α-helix	186-195	10
α-helix	208-229	22
β-strand	234-238	5	7
α-helix	239-244	6
α-helix	246-257	12
α-helix	263-266	4
β-strand	272	1	9
β-strand	278	1	9
α-helix	287-290	4
α-helix	293-294	2
α-helix	308-312	5
α-helix	314-317	4
α-helix	320-323	4

Chain D: 17 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	71-75	5	10
α-helix	82-90	9
β-strand	95-96	2	10
α-helix	103-116	14
α-helix	118-126	9
α-helix	131-148	18
β-strand	155-159	5	10
α-helix	161-166	6
α-helix	167-173	7
β-strand	178-183	6	10
α-helix	186-195	10
β-strand	200	1	11
α-helix	208-229	22
β-strand	234-238	5	10
α-helix	239-244	6
α-helix	246-256	11
α-helix	263-266	4
α-helix	268-271	4
β-strand	272	1	12
β-strand	278	1	12
α-helix	287-290	4
α-helix	293-294	2
α-helix	308-312	5
α-helix	314-317	4
α-helix	320-323	4

Chain L: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	1005	1	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein-tyrosine sulfotransferase 1	A, B, C, D	protein	303	Homo sapiens	O60507 (AlphaFold model)
gastrin peptide	F, H, J, L	protein	12	synthetic construct	P01350 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>5WRJ_1 Protein-tyrosine sulfotransferase 1 (chains A, B, C, D)
GSHMKLESTRTTVRTGLDLKANKTFAYHKDMPLIFIGGVPRSGTTLMRAMLDAHPDIRCG
EETRVIPRILALKQMWSRSSKEKIRLDEAGVTDEVLDSAMQAFLLEIIVKHGEPAPYLCN
KDPFALKSLTYLSRLFPNAKFLLMVRDGRASVHSMISRKVTIAGFDLNSYRDCLTKWNRA
IETMYNQCMEVGYKKCMLVHYEQLVLHPERWMRTLLKFLQIPWNHSVLHHEEMIGKAGGV
SLSKVERSTDQVIKPVNVGALSKWVGKIPPDVLQDMAVIAPMLAKLGYDPYANPPNYGKP
DPK

Sequence of entity 2 (F, H, J, L), FASTA

>5WRJ_2 gastrin peptide (chains F, H, J, L)
EEEEEAYGWMDF

Ligands and cofactors

ID	Name	Formula	Copies
A3P	Adenosine-3'-5'-diphosphate	C10 H15 N5 O10 P2	4
MG	Magnesium ion	Mg	4

Primary citation

Structural basis for the broad substrate specificity of the human tyrosylprotein sulfotransferase-1. Tanaka, S., Nishiyori, T., Kojo, H. et al. Sci Rep (2017) 7:8776-8776. DOI 10.1038/s41598-017-07141-8 · PubMed

Other PDB entries of the same protein (UniProt O60507 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5WRI 1.6 Å, Crystal structure of human tyrosylprotein sulfotransferase-1 complexed with PAP and C4…
9WP1 3.2 Å, Structural insights into tyrosine sulfation of CCR5 by human tyrosylprotein…

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