Structure of PDB 4qum Chain A

Receptor sequence
>4qumA (length=280) Species: 9606 (Homo sapiens) [Search protein sequence]
ADTLEGSMAQLKKGLESGTVLIQFEQLYRKKPGLAITFAKLPQNLDKNRY
KDVLPYDTTRVLLQGNEDYINASYVNMEIPAANLVNKYIATQGPLPHTCA
QFWQVVWDQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMNHGGFHIQCQS
EDCTIAYVSREMLVTNTQTGEEHTVTHLQYVAWPAHGVPDDSSDFLEFVN
YVRSLRVDSEPVLVHSSAGIGRTGVLVTMETAMCLTERNLPIYPLDIVRK
MRDQRAMMVQTSSQYKFVCEAILRVYEEGL
3D structure
PDB4qum Reciprocal allosteric regulation of p38 gamma and PTPN3 involves a PDZ domain-modulated complex formation.
ChainA
Resolution2.516 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) A811 S842 R848 T849 Q886
Catalytic site (residue number reindexed from 1) A185 S216 R222 T223 Q260
Enzyme Commision number 3.1.3.48: protein-tyrosine-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 N674 Y676 K677 D678 R751 H812 S842 S843 A844 I846 G847 R848 Q886 N48 Y50 K51 D52 R125 H186 S216 S217 A218 I220 G221 R222 Q260
Gene Ontology
Molecular Function
GO:0004725 protein tyrosine phosphatase activity
Biological Process
GO:0006470 protein dephosphorylation
GO:0016311 dephosphorylation

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:4qum, PDBe:4qum, PDBj:4qum
PDBsum4qum
PubMed25314968
UniProtP26045|PTN3_HUMAN Tyrosine-protein phosphatase non-receptor type 3 (Gene Name=PTPN3)

[Back to BioLiP]