Structure of PDB 6czo Chain C Binding Site BS02

Receptor Information
>6czo Chain C (length=293) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLEL
EAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETIC
LLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDC
FNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLL
WSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGY
EFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain6czo Chain C Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB6czo KNL1 Binding to PP1 and Microtubules Is Mutually Exclusive.
Resolution2.95 Å
Binding residue
(original residue number in PDB)
D64 H66 D92
Binding residue
(residue number reindexed from 1)
D59 H61 D87
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D64 H66 D92 D95 R96 N124 H125 H173 R221 H248
Catalytic site (residue number reindexed from 1) D59 H61 D87 D90 R91 N119 H120 H168 R216 H243
Enzyme Commision number 3.1.3.16: protein-serine/threonine phosphatase.
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity

View graph for
Molecular Function
External links
PDB RCSB:6czo, PDBe:6czo, PDBj:6czo
PDBsum6czo
PubMed30100357
UniProtP62136|PP1A_HUMAN Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (Gene Name=PPP1CA)

[Back to BioLiP]