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4JOB

Crystal structure of human lysophosphatidic acid phosphatase type 6 complexed with L-(+)-tartrate

Functional Information from GO Data
ChainGOidnamespacecontents
A0002244biological_processhematopoietic progenitor cell differentiation
A0003993molecular_functionacid phosphatase activity
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0006629biological_processlipid metabolic process
A0006644biological_processphospholipid metabolic process
A0006654biological_processphosphatidic acid biosynthetic process
A0016787molecular_functionhydrolase activity
A0052642molecular_functionlysophosphatidic acid phosphatase activity
A2001311biological_processlysobisphosphatidic acid metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE TLA A 501
ChainResidue
AARG58
AHIS59
AARG62
ALEU65
AARG168
AHIS334
AASP335

Functional Information from PROSITE/UniProt
site_idPS00616
Number of Residues15
DetailsHIS_ACID_PHOSPHAT_1 Histidine acid phosphatases phosphohistidine signature. LkmVqvVfRHGaRsP
ChainResidueDetails
ALEU50-PRO64

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:23807634
ChainResidueDetails
AHIS59

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:23807634
ChainResidueDetails
AASP335

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PDB entries from 2024-07-17

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