Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2HNX

Crystal Structure of aP2

Functional Information from GO Data
ChainGOidnamespacecontents
A0005324molecular_functionlong-chain fatty acid transmembrane transporter activity
A0005504molecular_functionfatty acid binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005811cellular_componentlipid droplet
A0005829cellular_componentcytosol
A0008289molecular_functionlipid binding
A0009617biological_processresponse to bacterium
A0015908biological_processfatty acid transport
A0015909biological_processlong-chain fatty acid transport
A0036041molecular_functionlong-chain fatty acid binding
A0042632biological_processcholesterol homeostasis
A0045892biological_processnegative regulation of DNA-templated transcription
A0050729biological_processpositive regulation of inflammatory response
A0050872biological_processwhite fat cell differentiation
A0050873biological_processbrown fat cell differentiation
A0051427molecular_functionhormone receptor binding
A0070062cellular_componentextracellular exosome
A0070343biological_processwhite fat cell proliferation
A0071285biological_processcellular response to lithium ion
A0071356biological_processcellular response to tumor necrosis factor
A0120162biological_processpositive regulation of cold-induced thermogenesis
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 A 137
ChainResidue
ASER13
AGLU14
AASN15
APHE16
AASP17
AHOH218
AHOH227
AHOH295
AHOH314

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PLM A 135
ChainResidue
APHE16
APRO38
ASER53
AASP76
AARG78
AARG126
ATYR128
AHOH210
AHOH247
AHOH265

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACY A 138
ChainResidue
ALYS21
AARG30
AARG108
AASP111
AARG130
AHOH341

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY A 140
ChainResidue
AILE51
ALYS52
ASER53
ATHR60
AHOH228

Functional Information from PROSITE/UniProt
site_idPS00214
Number of Residues18
DetailsFABP Cytosolic fatty-acid binding proteins signature. GTWkLvsSeNFDdYMKEV
ChainResidueDetails
AGLY6-VAL23

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsMotif: {"description":"Nuclear localization signal","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N-acetylcysteine","evidences":[{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P04117","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by Tyr-kinases","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

242500

PDB entries from 2025-10-01

PDB statisticsPDBj update infoContact PDBjnumon