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5ID9

Crystal structure of equine serum albumin in complex with phosphorodithioate derivative of myristoyl cyclic phosphatidic acid (cPA)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0005504molecular_functionfatty acid binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0008289molecular_functionlipid binding
A0009267biological_processcellular response to starvation
A0015643molecular_functiontoxic substance binding
A0019825molecular_functionoxygen binding
A0030170molecular_functionpyridoxal phosphate binding
A0032991cellular_componentprotein-containing complex
A0046872molecular_functionmetal ion binding
A0051902biological_processnegative regulation of mitochondrial depolarization
A0072732biological_processcellular response to calcium ion starvation
A1903981molecular_functionenterobactin binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue 6A4 A 601
ChainResidue
APHE205
AARG208
ATHR235
ALYS350
ALEU480
AALA481
AHOH754

site_idAC2
Number of Residues5
Detailsbinding site for residue MLI A 602
ChainResidue
ATHR428
AALA455
AARG458
AALA193
AGLU424

site_idAC3
Number of Residues5
Detailsbinding site for residue MLI A 603
ChainResidue
ALYS221
ALEU237
ASER286
AALA290
AHOH712

site_idAC4
Number of Residues8
Detailsbinding site for residue MLI A 604
ChainResidue
ALEU66
AHIS67
APHE70
AGLY247
AASP248
ALEU249
ALEU250
AGLU251

site_idAC5
Number of Residues1
Detailsbinding site for residue FMT A 605
ChainResidue
AHIS145

site_idAC6
Number of Residues2
Detailsbinding site for residue FMT A 606
ChainResidue
ALYS499
ALYS533

site_idAC7
Number of Residues3
Detailsbinding site for residue FMT A 608
ChainResidue
ALYS194
AARG217
AHOH741

Functional Information from PROSITE/UniProt
site_idPS00212
Number of Residues25
DetailsALBUMIN_1 Albumin domain signature. YkadfteCCpaDdkagCLipkldaL
ChainResidueDetails
ATYR160-LEU184
ATYR352-PHE376
APHE550-LEU574

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P02770
ChainResidueDetails
AHIS3

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P02769
ChainResidueDetails
AGLU251
AASP254
AASP258
AASP13
AGLU243
AGLU6

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:28567254, ECO:0007744|PDB:5IIH
ChainResidueDetails
AHIS67
AHIS246
AASP248

site_idSWS_FT_FI4
Number of Residues5
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P02768
ChainResidueDetails
ASER58
ASER65
ASER418
ASER488
ASER5

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P02768
ChainResidueDetails
ATHR419
ATHR421
ATHR83

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P02768
ChainResidueDetails
ALYS533

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P02770
ChainResidueDetails
ATHR545

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P07724
ChainResidueDetails
ALYS563

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PDB entries from 2024-06-12

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