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5FUO

Extending the half-life of a Fab fragment through generation of a humanised anti-Human Serum Albumin (HSA) Fv domain: an investigation into the correlation between affinity and serum half-life

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0005504molecular_functionfatty acid binding
A0005507molecular_functioncopper ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005788cellular_componentendoplasmic reticulum lumen
A0005794cellular_componentGolgi apparatus
A0008289molecular_functionlipid binding
A0009267biological_processcellular response to starvation
A0015643molecular_functiontoxic substance binding
A0016209molecular_functionantioxidant activity
A0019825molecular_functionoxygen binding
A0030170molecular_functionpyridoxal phosphate binding
A0031093cellular_componentplatelet alpha granule lumen
A0032991cellular_componentprotein-containing complex
A0036094molecular_functionsmall molecule binding
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0051087molecular_functionprotein-folding chaperone binding
A0051902biological_processnegative regulation of mitochondrial depolarization
A0070062cellular_componentextracellular exosome
A0072562cellular_componentblood microparticle
A0072732biological_processcellular response to calcium ion starvation
A0098869biological_processcellular oxidant detoxification
A0140272molecular_functionexogenous protein binding
A1903981molecular_functionenterobactin binding
Functional Information from PROSITE/UniProt
site_idPS00212
Number of Residues25
DetailsALBUMIN_1 Albumin domain signature. YkaafteCCqaAdkaaCLlpkldeL
ChainResidueDetails
ATYR161-LEU185
ATYR353-PHE377
APHE551-LEU575

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH
ChainResidueDetails
HTYR202-HIS208
LTYR195-HIS201

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
AGLU252
AASP255
AASP259
AGLU6
AASP13
AGLU244

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:28567254, ECO:0007744|PDB:5IJF
ChainResidueDetails
AHIS67
AHIS247
AASP249

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:656055
ChainResidueDetails
ALYS240

site_idSWS_FT_FI5
Number of Residues37
DetailsSITE: Not glycated => ECO:0000269|PubMed:15047055
ChainResidueDetails
ALYS20
ALYS41
ALYS64
ALYS73
ALYS93
ALYS106
ALYS136
ALYS159
ALYS174
ALYS181
ALYS190
ALYS195
ALYS205
ALYS212
ALYS240
ALYS262
ALYS274
ALYS286
ALYS359
ALYS372
ALYS389
ALYS402
ALYS414
ALYS432
ALYS436
ALYS466
ALYS475
ALYS500
ALYS519
ALYS524
ALYS538
ALYS541
ALYS557
ALYS560
ALYS564
ALYS574
ALYS4

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Aspirin-acetylated lysine
ChainResidueDetails
ALYS199

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039
ChainResidueDetails
ASER5

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER58

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER65

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by FAM20C => ECO:0000269|PubMed:26091039
ChainResidueDetails
ATHR83

site_idSWS_FT_FI11
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P07724
ChainResidueDetails
ALYS436
ALYS519
ALYS564
ALYS205

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07724
ChainResidueDetails
ASER273

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ASER419

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ATHR420
ATHR422

site_idSWS_FT_FI15
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER489

site_idSWS_FT_FI16
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0007744|PubMed:24129315
ChainResidueDetails
ALYS534

site_idSWS_FT_FI17
Number of Residues4
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:3759977
ChainResidueDetails
ALYS317
ALYS439
ALYS12
ALYS281

site_idSWS_FT_FI18
Number of Residues13
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055
ChainResidueDetails
ALYS137
ALYS162
ALYS225
ALYS276
ALYS313
ALYS323
ALYS378
ALYS413
ALYS444
ALYS536
ALYS545
ALYS573
ALYS51

site_idSWS_FT_FI19
Number of Residues1
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:3759977, ECO:0000269|PubMed:6853480
ChainResidueDetails
ALYS199

site_idSWS_FT_FI20
Number of Residues2
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:15047055, ECO:0000269|PubMed:3759977
ChainResidueDetails
ALYS233
ALYS351

site_idSWS_FT_FI21
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; in variant Redhill
ChainResidueDetails
AASN318

site_idSWS_FT_FI22
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; in variant Casebrook
ChainResidueDetails
AASP494

site_idSWS_FT_FI23
Number of Residues1
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:15047055, ECO:0000269|PubMed:3759977, ECO:0000269|PubMed:6706980, ECO:0000269|PubMed:6853480
ChainResidueDetails
ALYS525

site_idSWS_FT_FI24
Number of Residues1
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:3759977
ChainResidueDetails
ALYS534

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PDB entries from 2024-04-17

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