Structure of PDB 4xpn Chain A

Receptor sequence
>4xpnA (length=296) Species: 9606 (Homo sapiens) [Search protein sequence]
MGSLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILL
ELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLET
ICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFT
DCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCD
LLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVED
GYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPA
3D structure
PDB4xpn Structural and Functional Analysis of the GADD34:PP1 eIF2 alpha Phosphatase.
ChainA
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) D61 H63 D89 D92 R93 N121 H122 H170 R218 H245
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 A Y78 D166 D242 F257 R261 E287 T288 L289 M290 C291 Q294 I295 K297 Y75 D163 D239 F254 R258 E284 T285 L286 M287 C288 Q291 I292 K294
BS02 MN A D64 H66 D92 D61 H63 D89
BS03 MN A D92 N124 H173 H248 D89 N121 H170 H245
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]