Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8HQ1

Crystal Structure Of Human Lgi1-Adam22 Complex In Space Group C2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004222	molecular_function	metalloendopeptidase activity
A	0006508	biological_process	proteolysis
A	0008237	molecular_function	metallopeptidase activity
B	0004222	molecular_function	metalloendopeptidase activity
B	0006508	biological_process	proteolysis
B	0008237	molecular_function	metallopeptidase activity
C	0004222	molecular_function	metalloendopeptidase activity
C	0006508	biological_process	proteolysis
C	0008237	molecular_function	metallopeptidase activity
D	0005102	molecular_function	signaling receptor binding
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0005615	cellular_component	extracellular space
D	0005737	cellular_component	cytoplasm
D	0005783	cellular_component	endoplasmic reticulum
D	0005794	cellular_component	Golgi apparatus
D	0007165	biological_process	signal transduction
D	0007399	biological_process	nervous system development
D	0007411	biological_process	axon guidance
D	0030307	biological_process	positive regulation of cell growth
D	0030425	cellular_component	dendrite
D	0031175	biological_process	neuron projection development
D	0043083	cellular_component	synaptic cleft
D	0043194	cellular_component	axon initial segment
D	0045202	cellular_component	synapse
D	0048018	molecular_function	receptor ligand activity
D	0050806	biological_process	positive regulation of synaptic transmission
D	0098978	cellular_component	glutamatergic synapse
D	0099645	biological_process	neurotransmitter receptor localization to postsynaptic specialization membrane
E	0005102	molecular_function	signaling receptor binding
E	0005515	molecular_function	protein binding
E	0005576	cellular_component	extracellular region
E	0005615	cellular_component	extracellular space
E	0005737	cellular_component	cytoplasm
E	0005783	cellular_component	endoplasmic reticulum
E	0005794	cellular_component	Golgi apparatus
E	0007165	biological_process	signal transduction
E	0007399	biological_process	nervous system development
E	0007411	biological_process	axon guidance
E	0030307	biological_process	positive regulation of cell growth
E	0030425	cellular_component	dendrite
E	0031175	biological_process	neuron projection development
E	0043083	cellular_component	synaptic cleft
E	0043194	cellular_component	axon initial segment
E	0045202	cellular_component	synapse
E	0048018	molecular_function	receptor ligand activity
E	0050806	biological_process	positive regulation of synaptic transmission
E	0098978	cellular_component	glutamatergic synapse
E	0099645	biological_process	neurotransmitter receptor localization to postsynaptic specialization membrane
F	0005102	molecular_function	signaling receptor binding
F	0005515	molecular_function	protein binding
F	0005576	cellular_component	extracellular region
F	0005615	cellular_component	extracellular space
F	0005737	cellular_component	cytoplasm
F	0005783	cellular_component	endoplasmic reticulum
F	0005794	cellular_component	Golgi apparatus
F	0007165	biological_process	signal transduction
F	0007399	biological_process	nervous system development
F	0007411	biological_process	axon guidance
F	0030307	biological_process	positive regulation of cell growth
F	0030425	cellular_component	dendrite
F	0031175	biological_process	neuron projection development
F	0043083	cellular_component	synaptic cleft
F	0043194	cellular_component	axon initial segment
F	0045202	cellular_component	synapse
F	0048018	molecular_function	receptor ligand activity
F	0050806	biological_process	positive regulation of synaptic transmission
F	0098978	cellular_component	glutamatergic synapse
F	0099645	biological_process	neurotransmitter receptor localization to postsynaptic specialization membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue CA A 804

Chain	Residue
A	GLU242
A	ASP325
A	CYS433
A	ASN436

site_id	AC2
Number of Residues	6
Details	binding site for residue CA A 805

Chain	Residue
A	ASP459
A	GLU446
A	ASN449
A	PHE451
A	GLU453
A	GLU456

site_id	AC3
Number of Residues	5
Details	binding site for residue CA A 806

Chain	Residue
A	ASP511
A	ILE512
A	GLU514
A	ASN526
A	ILE527

site_id	AC4
Number of Residues	5
Details	binding site for residue CA B 804

Chain	Residue
B	ASP511
B	ILE512
B	GLU514
B	ASN526
B	ILE527

site_id	AC5
Number of Residues	4
Details	binding site for residue CA B 805

Chain	Residue
B	GLU242
B	ASP325
B	CYS433
B	ASN436

site_id	AC6
Number of Residues	6
Details	binding site for residue CA B 806

Chain	Residue
B	GLU446
B	ASN449
B	PHE451
B	GLU453
B	GLU456
B	ASP459

site_id	AC7
Number of Residues	5
Details	binding site for residue CA C 804

Chain	Residue
C	ASP511
C	ILE512
C	GLU514
C	ASN526
C	ILE527

site_id	AC8
Number of Residues	4
Details	binding site for residue CA C 805

Chain	Residue
C	GLU242
C	ASP325
C	CYS433
C	ASN436

site_id	AC9
Number of Residues	7
Details	binding site for residue CA C 806

Chain	Residue
C	GLU446
C	CYS447
C	ASN449
C	PHE451
C	GLU453
C	GLU456
C	ASP459

site_id	AD1
Number of Residues	5
Details	binding site for residue CA D 604

Chain	Residue
D	ASP334
D	ASP381
D	VAL382
D	GLU383
D	LYS436

site_id	AD2
Number of Residues	6
Details	binding site for residue CA E 604

Chain	Residue
E	ASP334
E	GLU336
E	ASP381
E	VAL382
E	GLU383
E	LYS436

site_id	AD3
Number of Residues	6
Details	binding site for residue CA F 604

Chain	Residue
F	ASP334
F	GLU336
F	ASP381
F	VAL382
F	GLU383
F	LYS436

site_id	AD4
Number of Residues	2
Details	binding site for Mono-Saccharide NAG A 801 bound to ASN A 519

Chain	Residue
A	SER517
A	ASN519

site_id	AD5
Number of Residues	4
Details	binding site for Mono-Saccharide NAG A 803 bound to ASN A 634

Chain	Residue
A	SER623
A	LEU625
A	ASN634
A	SER636

site_id	AD6
Number of Residues	5
Details	binding site for Mono-Saccharide NAG A 802 bound to ASN A 675

Chain	Residue
A	ASN675
C	LEU352
C	LYS353
C	ASP653
C	LEU664

site_id	AD7
Number of Residues	1
Details	binding site for Mono-Saccharide NAG B 801 bound to ASN B 519

Chain	Residue
B	ASN519

site_id	AD8
Number of Residues	4
Details	binding site for Mono-Saccharide NAG B 803 bound to ASN B 634

Chain	Residue
B	ASN607
B	SER623
B	LEU625
B	ASN634

site_id	AD9
Number of Residues	1
Details	binding site for Mono-Saccharide NAG B 802 bound to ASN B 675

Chain	Residue
B	ASN675

site_id	AE1
Number of Residues	2
Details	binding site for Mono-Saccharide NAG C 801 bound to ASN C 519

Chain	Residue
C	SER517
C	ASN519

site_id	AE2
Number of Residues	1
Details	binding site for Mono-Saccharide NAG C 803 bound to ASN C 634

Chain	Residue
C	ASN634

site_id	AE3
Number of Residues	1
Details	binding site for Mono-Saccharide NAG C 802 bound to ASN C 675

Chain	Residue
C	ASN675

site_id	AE4
Number of Residues	1
Details	binding site for Mono-Saccharide NAG D 602 bound to ASN D 192

Chain	Residue
D	ASN192

site_id	AE5
Number of Residues	5
Details	binding site for Mono-Saccharide NAG D 603 bound to ASN D 277

Chain	Residue
D	LYS259
D	ASN274
D	TYR275
D	ASP276
D	ASN277

site_id	AE6
Number of Residues	1
Details	binding site for Mono-Saccharide NAG D 601 bound to ASN D 422

Chain	Residue
D	ASN422

site_id	AE7
Number of Residues	2
Details	binding site for Mono-Saccharide NAG E 602 bound to ASN E 192

Chain	Residue
E	HIS190
E	ASN192

site_id	AE8
Number of Residues	3
Details	binding site for Mono-Saccharide NAG E 603 bound to ASN E 277

Chain	Residue
E	LYS259
E	ILE261
E	ASN277

site_id	AE9
Number of Residues	2
Details	binding site for Mono-Saccharide NAG E 601 bound to ASN E 422

Chain	Residue
E	ASN422
E	GLN423

site_id	AF1
Number of Residues	3
Details	binding site for Mono-Saccharide NAG F 602 bound to ASN F 192

Chain	Residue
F	ASP163
F	ASN192
F	LEU162

site_id	AF2
Number of Residues	3
Details	binding site for Mono-Saccharide NAG F 603 bound to ASN F 277

Chain	Residue
F	LYS259
F	ASN274
F	ASN277

site_id	AF3
Number of Residues	5
Details	binding site for Mono-Saccharide NAG F 601 bound to ASN F 422

Chain	Residue
F	ARG389
F	GLN412
F	ASN422
F	GLN423
F	THR424

Functional Information from PROSITE/UniProt

site_id	PS00022
Number of Residues	12
Details	EGF_1 EGF-like domain signature 1. CvCnrHwiGSdC

Chain	Residue	Details
A	CYS700-CYS711

site_id	PS00427
Number of Residues	20
Details	DISINTEGRIN_1 Disintegrins signature. CsdGlCCk.KCkFqpmgtvCR

Chain	Residue	Details
A	CYS485-ARG504

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	597
Details	Domain: {"description":"Peptidase M12B","evidences":[{"source":"PROSITE-ProRule","id":"PRU00276","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	261
Details	Domain: {"description":"Disintegrin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00068","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	111
Details	Domain: {"description":"EGF-like"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	9
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19692335","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	63
Details	Repeat: {"description":"LRR 1"}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	63
Details	Repeat: {"description":"LRR 2"}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	63
Details	Repeat: {"description":"LRR 3"}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	150
Details	Domain: {"description":"LRRCT"}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	126
Details	Repeat: {"description":"EAR 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00075","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	126
Details	Repeat: {"description":"EAR 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00075","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	141
Details	Repeat: {"description":"EAR 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00075","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	147
Details	Repeat: {"description":"EAR 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00075","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	129
Details	Repeat: {"description":"EAR 5","evidences":[{"source":"PROSITE-ProRule","id":"PRU00075","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	126
Details	Repeat: {"description":"EAR 6","evidences":[{"source":"PROSITE-ProRule","id":"PRU00075","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	126
Details	Repeat: {"description":"EAR 7","evidences":[{"source":"PROSITE-ProRule","id":"PRU00075","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	9
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)