Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6AQ1

The crystal structure of human FABP3

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008092molecular_functioncytoskeletal protein binding
A0008285biological_processnegative regulation of cell population proliferation
A0008289molecular_functionlipid binding
A0015909biological_processlong-chain fatty acid transport
A0032365biological_processintracellular lipid transport
A0036041molecular_functionlong-chain fatty acid binding
A0042632biological_processcholesterol homeostasis
A0046320biological_processregulation of fatty acid oxidation
A0050873biological_processbrown fat cell differentiation
A0055091biological_processphospholipid homeostasis
A0070062cellular_componentextracellular exosome
A0070538molecular_functionoleic acid binding
A0071073biological_processpositive regulation of phospholipid biosynthetic process
A0140214biological_processpositive regulation of long-chain fatty acid import into cell
A2001245biological_processregulation of phosphatidylcholine biosynthetic process
B0005515molecular_functionprotein binding
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008092molecular_functioncytoskeletal protein binding
B0008285biological_processnegative regulation of cell population proliferation
B0008289molecular_functionlipid binding
B0015909biological_processlong-chain fatty acid transport
B0032365biological_processintracellular lipid transport
B0036041molecular_functionlong-chain fatty acid binding
B0042632biological_processcholesterol homeostasis
B0046320biological_processregulation of fatty acid oxidation
B0050873biological_processbrown fat cell differentiation
B0055091biological_processphospholipid homeostasis
B0070062cellular_componentextracellular exosome
B0070538molecular_functionoleic acid binding
B0071073biological_processpositive regulation of phospholipid biosynthetic process
B0140214biological_processpositive regulation of long-chain fatty acid import into cell
B2001245biological_processregulation of phosphatidylcholine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue SO4 A 201
ChainResidue
ASER14
BASP78
ALYS15
AASN16
APHE17
AASP18
AHOH352
AHOH412
AHOH428
BLYS59

site_idAC2
Number of Residues6
Detailsbinding site for residue PLM A 202
ChainResidue
AMET21
ALEU116
AARG127
ATYR129
AHOH311
AHOH334

site_idAC3
Number of Residues10
Detailsbinding site for residue SO4 B 201
ChainResidue
BSER14
BLYS15
BASN16
BPHE17
BASP18
BSER35
BHOH313
BHOH330
BHOH368
BHOH393

site_idAC4
Number of Residues6
Detailsbinding site for residue SO4 B 202
ChainResidue
BGLY27
BPHE28
BARG31
BHOH358
BHOH420
BHOH424

site_idAC5
Number of Residues5
Detailsbinding site for residue SO4 B 203
ChainResidue
ALYS113
BLYS53
BHIS55
BHOH305
BHOH306

site_idAC6
Number of Residues10
Detailsbinding site for residue PLM B 204
ChainResidue
BTHR37
BTHR54
BSER56
BPHE58
BASP77
BLEU116
BARG127
BTYR129
BHOH322
BHOH345

Functional Information from PROSITE/UniProt
site_idPS00214
Number of Residues18
DetailsFABP Cytosolic fatty-acid binding proteins signature. GTWkLvdSkNFDdYMKSL
ChainResidueDetails
AGLY7-LEU24

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:7922029, ECO:0007744|PDB:1HMT
ChainResidueDetails
BARG127
AARG127

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylvaline => ECO:0007744|PubMed:22223895
ChainResidueDetails
AVAL2
BVAL2

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P07483
ChainResidueDetails
BTHR8
BTHR30
ATHR8
ATHR30

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by Tyr-kinases => ECO:0000250|UniProtKB:P07483
ChainResidueDetails
BTYR20
ATYR20

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07483
ChainResidueDetails
ASER23
ASER83
BSER23
BSER83

219869

PDB entries from 2024-05-15

PDB statisticsPDBj update infoContact PDBjnumon