Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6T6R

Human endoplasmic reticulum aminopeptidase 1 (ERAP1) in complex with (4aR,5S,6R,8S,8aR)-5-(2-(Furan-3-yl)ethyl)-8-hydroxy-5,6,8a-trimethyl-3,4,4a,5,6,7,8,8a-octahydronaphthalene-1-carboxylic acid

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001525	biological_process	angiogenesis
A	0002250	biological_process	adaptive immune response
A	0002376	biological_process	immune system process
A	0002474	biological_process	antigen processing and presentation of peptide antigen via MHC class I
A	0004175	molecular_function	endopeptidase activity
A	0004177	molecular_function	aminopeptidase activity
A	0005138	molecular_function	interleukin-6 receptor binding
A	0005151	molecular_function	interleukin-1, type II receptor binding
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005737	cellular_component	cytoplasm
A	0005783	cellular_component	endoplasmic reticulum
A	0005788	cellular_component	endoplasmic reticulum lumen
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0005829	cellular_component	cytosol
A	0006508	biological_process	proteolysis
A	0006509	biological_process	membrane protein ectodomain proteolysis
A	0008217	biological_process	regulation of blood pressure
A	0008233	molecular_function	peptidase activity
A	0008235	molecular_function	metalloexopeptidase activity
A	0008237	molecular_function	metallopeptidase activity
A	0008270	molecular_function	zinc ion binding
A	0009617	biological_process	response to bacterium
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0019885	biological_process	antigen processing and presentation of endogenous peptide antigen via MHC class I
A	0043171	biological_process	peptide catabolic process
A	0045088	biological_process	regulation of innate immune response
A	0045444	biological_process	fat cell differentiation
A	0046872	molecular_function	metal ion binding
A	0070006	molecular_function	metalloaminopeptidase activity
A	0070062	cellular_component	extracellular exosome
A	1905368	cellular_component	peptidase complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN A 1001

Chain	Residue
A	HIS353
A	HIS357
A	GLU376
A	MLT1002

site_id	AC2
Number of Residues	13
Details	binding site for residue MLT A 1002

Chain	Residue
A	HIS357
A	GLU376
A	TYR438
A	ZN1001
A	HOH1101
A	HOH1220
A	HOH1231
A	HOH1300
A	GLY317
A	ALA318
A	GLU320
A	HIS353
A	GLU354

site_id	AC3
Number of Residues	9
Details	binding site for residue MLT A 1003

Chain	Residue
A	LYS81
A	ARG108
A	GLU117
A	VAL148
A	HIS150
A	HOH1183
A	HOH1213
A	HOH1359
A	HOH1436

site_id	AC4
Number of Residues	6
Details	binding site for residue EDO A 1004

Chain	Residue
A	PRO682
A	TRP921
A	HOH1175
A	HOH1461
A	HOH1636
A	HOH1696

site_id	AC5
Number of Residues	6
Details	binding site for residue EDO A 1005

Chain	Residue
A	SER340
A	ALA341
A	SER342
A	SER729
A	ASP766
A	HOH1661

site_id	AC6
Number of Residues	7
Details	binding site for residue EDO A 1006

Chain	Residue
A	ARG690
A	MET922
A	ASP923
A	PHE926
A	HOH1238
A	HOH1354
A	HOH1670

site_id	AC7
Number of Residues	8
Details	binding site for residue EDO A 1007

Chain	Residue
A	GLU118
A	ALA776
A	GLN777
A	THR779
A	THR808
A	ASN810
A	HOH1289
A	HOH1307

site_id	AC8
Number of Residues	7
Details	binding site for residue EDO A 1008

Chain	Residue
A	ARG430
A	PHE433
A	SER868
A	SER869
A	EDO1011
A	HOH1118
A	HOH1166

site_id	AC9
Number of Residues	6
Details	binding site for residue EDO A 1009

Chain	Residue
A	GLU129
A	THR185
A	MET189
A	ARG430
A	GLU865
A	HOH1346

site_id	AD1
Number of Residues	6
Details	binding site for residue EDO A 1010

Chain	Residue
A	GLN181
A	SER316
A	ALA318
A	MET319
A	EDO1011
A	HOH1618

site_id	AD2
Number of Residues	5
Details	binding site for residue EDO A 1011

Chain	Residue
A	TYR438
A	EDO1008
A	EDO1010
A	EDO1013
A	HOH1231

site_id	AD3
Number of Residues	5
Details	binding site for residue EDO A 1012

Chain	Residue
A	SER416
A	HIS417
A	PRO418
A	ARG906
A	HOH1379

site_id	AD4
Number of Residues	8
Details	binding site for residue EDO A 1013

Chain	Residue
A	GLN315
A	SER316
A	SER869
A	SER870
A	HIS873
A	EDO1011
A	HOH1118
A	HOH1370

site_id	AD5
Number of Residues	5
Details	binding site for residue EDO A 1014

Chain	Residue
A	SER453
A	ARG854
A	ASN858
A	HOH1602
A	HOH1658

site_id	AD6
Number of Residues	2
Details	binding site for residue EDO A 1015

Chain	Residue
A	ARG328
A	HOH1279

site_id	AD7
Number of Residues	7
Details	binding site for residue EDO A 1016

Chain	Residue
A	GLN428
A	GLU431
A	ARG906
A	HOH1127
A	HOH1495
A	THR421
A	VAL423

site_id	AD8
Number of Residues	6
Details	binding site for residue EDO A 1017

Chain	Residue
A	THR668
A	GLU669
A	ILE670
A	SER723
A	GLU724
A	HOH1634

site_id	AD9
Number of Residues	7
Details	binding site for residue EDO A 1018

Chain	Residue
A	TYR296
A	ARG449
A	ALA454
A	ASP455
A	LYS458
A	HOH1256
A	HOH1734

site_id	AE1
Number of Residues	7
Details	binding site for residue EDO A 1019

Chain	Residue
A	ALA69
A	LEU71
A	ARG209
A	GLU210
A	HIS213
A	ILE251
A	HOH1162

site_id	AE2
Number of Residues	4
Details	binding site for residue EDO A 1020

Chain	Residue
A	MET576
A	VAL577
A	ARG854
A	HOH1218

site_id	AE3
Number of Residues	6
Details	binding site for residue EDO A 1021

Chain	Residue
A	LYS164
A	ASP313
A	LYS863
A	HOH1102
A	HOH1234
A	HOH1554

site_id	AE4
Number of Residues	11
Details	binding site for residue MNZ A 1022

Chain	Residue
A	PHE674
A	LEU677
A	ASN678
A	ILE681
A	TYR684
A	LYS685
A	GLN730
A	ARG807
A	HOH1217
A	HOH1448
A	HOH1544

Functional Information from PROSITE/UniProt

site_id	PS00142
Number of Residues	10
Details	ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TVAHELAHQW

Chain	Residue	Details
A	THR350-TRP359

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	5
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	3
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
Details	Site: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"21478864","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of the soluble domain of human endoplasmic reticulum aminopeptidase 1 ERAP1.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of the soluble domain of human endoplasmic reticulum aminopeptidase 1 ERAP1.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"21478864","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)