Structure of PDB 4xpn Chain C

Receptor sequence
>4xpnC (length=294) Species: 9606 (Homo sapiens) [Search protein sequence]
SLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLEL
EAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETIC
LLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDC
FNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLL
WSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGY
EFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPA
3D structure
PDB4xpn Structural and Functional Analysis of the GADD34:PP1 eIF2 alpha Phosphatase.
ChainC
Resolution2.285 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 peptide C Y78 D166 D242 L243 F257 E287 T288 L289 M290 C291 F293 Q294 I295 K297 Y73 D161 D237 L238 F252 E282 T283 L284 M285 C286 F288 Q289 I290 K292
BS02 MN C D92 N124 H173 H248 D87 N119 H168 H243
BS03 MN C D64 H66 D92 D59 H61 D87
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity

View graph for
Molecular Function
External links
PDB RCSB:4xpn, PDBe:4xpn, PDBj:4xpn
PDBsum4xpn
PubMed26095357
UniProtP62136|PP1A_HUMAN Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (Gene Name=PPP1CA)

[Back to BioLiP]