3L0C: PDB entry 3L0C

Crystal structure of SCP1 phosphatase D206A mutant with trapped inorganic phosphate. Determined by X-ray diffraction at 2.45 Å resolution. Released 23 Mar 2010.

Method: X-ray diffraction
Resolution: 2.45 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,946
Mol. weight: 42.31 kDa
Ligands: MG, PO4
Released: 23 Mar 2010

Explore 3L0C in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3L0C contains 28 α-helices and 22 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: 13 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	81-84	4
α-helix	85-88	4
α-helix	91	1
β-strand	92-95	4	1
β-strand	98	1	2
β-strand	102-105	4	2
β-strand	114-120	7	2
β-strand	123-131	9	2
α-helix	132	1
α-helix	135-145	11
β-strand	147-151	5	1
α-helix	156-166	11
β-strand	172-176	5	1
α-helix	178-180	3
β-strand	182-184	3	3
β-strand	187-189	3	3
α-helix	192-194	3
α-helix	199-201	3
β-strand	202-206	5	1
α-helix	209-212	4
α-helix	216-218	3
β-strand	219-221	3	1
α-helix	233-246	14
α-helix	250-252	3

Chain B: 15 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	83-84	2
α-helix	85-87	3
α-helix	91	1
β-strand	92-95	4	4
β-strand	98	1	5
β-strand	102-105	4	5
β-strand	114-120	7	5
β-strand	123-131	9	5
α-helix	132	1
α-helix	135-145	11
β-strand	147-151	5	4
α-helix	156-166	11
β-strand	172-176	5	4
α-helix	178-180	3
β-strand	182-184	3	6
β-strand	187-189	3	6
α-helix	192-194	3
α-helix	199-201	3
β-strand	202-206	5	4
α-helix	209-212	4
α-helix	216-218	3
β-strand	219-221	3	4
α-helix	223-225	3
α-helix	233-236	4
α-helix	238-244	7
α-helix	250-252	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1	A, B	protein	184	Homo sapiens	Q9GZU7 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3L0C_1 Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1 (chains A, B)
GSHGQYLLPEAKAQDSDKICVVIDLDETLVHSSFKPVNNADFIIPVEIDGVVHQVYVLKR
PHVDEFLQRMGELFECVLFTASLAKYADPVADLLDKWGAFRARLFRESCVFHRGNYVKDL
SRLGRDLRRVLILANSPASYVFHPDNAVPVASWFDNMSDTELHDLLPFFEQLSRVDDVYS
VLRQ

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	2
PO4	Phosphate ion	O4 P	2

Primary citation

Structural and functional analysis of the phosphoryl transfer reaction mediated by the human small C-terminal domain phosphatase, Scp1. Zhang, M., Liu, J., Kim, Y. et al. Protein Sci (2010) 19:974-986. DOI 10.1002/pro.375 · PubMed

Other PDB entries of the same protein (UniProt Q9GZU7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2GHT 1.8 Å, CTD-specific phosphatase Scp1 in complex with peptide from C-terminal domain of RNA…
2GHQ 2.05 Å, CTD-specific phosphatase Scp1 in complex with peptide C-terminal domain of RNA…
1TA0 2.1 Å, Three-dimensional structure of a RNA-polymerase II binding protein with associated ligand.
4YH1 2.2 Å, Structure of Human Scp1 bound to cis-proline peptidomimetic CTD phospho-Ser5 peptide
1T9Z 2.3 Å, Three-dimensional structure of a RNA-polymerase II binding protein.
3L0Y 2.3 Å, Crystal structure OF SCP1 phosphatase D98A mutant
3L0B 2.35 Å, Crystal structure of SCP1 phosphatase D206A mutant phosphoryl-intermediate
3PGL 2.35 Å, Crystal structure of human small C-terminal domain phosphatase 1 (Scp1) bound to…
4YGY 2.36 Å, Crystal Structure of Human Scp1 bound to trans-proline peptidomimetic CTD phospho-Ser5…
6DU3 2.58 Å, Structure of Scp1 D96N bound to REST-pS861/4 peptide

Browse structure collections

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