Structure of PDB 8itr Chain A

Receptor sequence

>8itrA (length=582) Species: 9606 (Homo sapiens) [Search protein sequence]

HKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKT
CVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECF
LQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAP
ELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCAS
LQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLE
CADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADL
PSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKT
YETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYK
FQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDY
LSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEF
NAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFA
AFVEKCCKADDKETCFAEEGKKLVAASQAALG

3D structure

PDB

8itr Crystal structures of human serum albumin in complex with lysophosphatidylcholine.

Chain

Resolution

2.44 Å

3D
structure

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Enzymatic activity

Enzyme Commision number

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	LPC	A	Q196 K199 W214 R218 L219 H242 I264 I290 A291	Q194 K197 W212 R216 L217 H240 I262 I288 A289
BS02	LPC	A	R117 L135 Y138 L139 I142 F149 F157 A158 Y161 F165 R186 G189	R115 L133 Y136 L137 I140 F147 F155 A156 Y159 F163 R184 G187
BS03	LPC	A	L22 V46 F49 L69 F70 Y150 A254 A258 L284 S287	L20 V44 F47 L67 F68 Y148 A252 A256 L282 S285
BS04	LPC	A	S342 V344 R348 L387 N391 Y411 V482 R484 R485 F488	S340 V342 R346 L385 N389 Y409 V480 R482 R483 F486
BS05	LPC	A	Y401 F507 K525 A528 L529 F551 A552 V555	Y399 F505 K523 A526 L527 F549 A550 V553
BS06	LPC	A	F206 R209 A210 K212 S232	F204 R207 A208 K210 S230

Gene Ontology

	Molecular Function
GO:0003677	DNA binding
GO:0005504	fatty acid binding
GO:0005507	copper ion binding
GO:0005515	protein binding
GO:0008289	lipid binding
GO:0015643	toxic substance binding
GO:0016209	antioxidant activity
GO:0019825	oxygen binding
GO:0030170	pyridoxal phosphate binding
GO:0042802	identical protein binding
GO:0046872	metal ion binding
GO:0051087	protein-folding chaperone binding
GO:0140272	exogenous protein binding
GO:1903981	enterobactin binding

	Biological Process
GO:0009267	cellular response to starvation
GO:0051902	negative regulation of mitochondrial depolarization
GO:0072732	cellular response to calcium ion starvation
GO:0098869	cellular oxidant detoxification

	Cellular Component
GO:0005576	extracellular region
GO:0005615	extracellular space
GO:0005634	nucleus
GO:0005737	cytoplasm
GO:0005783	endoplasmic reticulum
GO:0005788	endoplasmic reticulum lumen
GO:0005794	Golgi apparatus
GO:0031093	platelet alpha granule lumen
GO:0032991	protein-containing complex
GO:0070062	extracellular exosome
GO:0072562	blood microparticle

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:8itr, PDBe:8itr, PDBj:8itr
PDBsum	8itr
PubMed	37731243
UniProt	P02768\|ALBU_HUMAN Albumin (Gene Name=ALB)

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