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4TKB

The 0.86 angstrom X-ray structure of the human heart fatty acid-binding protein complexed with lauric acid

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
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue DAO A 200
ChainResidue
ATHR29
APHE57
ALYS58
AALA75
ALEU115
AARG126
ATYR128
AHOH449
AHOH454

site_idAC2
Number of Residues13
Detailsbinding site for residue P6G A 201
ChainResidue
AVAL11
ASER34
AMET35
ATHR36
ALYS37
APHE70
AASP71
AGLY120
ATHR121
AHOH319
AHOH325
AHOH342
AHOH472

site_idAC3
Number of Residues6
Detailsbinding site for residue P6G A 202
ChainResidue
AGLN31
AASP47
ALYS65
AGLY111
AHOH386
AHOH413

Functional Information from PROSITE/UniProt
site_idPS00214
Number of Residues18
DetailsFABP Cytosolic fatty-acid binding proteins signature. GTWkLvdSkNFDdYMKSL
ChainResidueDetails
AGLY6-LEU23

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:7922029, ECO:0007744|PDB:1HMT
ChainResidueDetails
AARG126

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylvaline => ECO:0007744|PubMed:22223895
ChainResidueDetails
AVAL1

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P07483
ChainResidueDetails
ATHR7
ATHR29

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by Tyr-kinases => ECO:0000250|UniProtKB:P07483
ChainResidueDetails
ATYR19

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07483
ChainResidueDetails
ASER22
ASER82

224004

PDB entries from 2024-08-21

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