Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8HQ2

Crystal structure of human ADAM22 in complex with human LGI1 mutant

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
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue CA A 801

Chain	Residue
A	ASP325
A	CYS433
A	ASN436

site_id	AC2
Number of Residues	6
Details	binding site for residue CA A 802

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

site_id	AC3
Number of Residues	5
Details	binding site for residue CA A 803

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

site_id	AC4
Number of Residues	4
Details	binding site for residue CA D 601

Chain	Residue
D	ASP334
D	GLU336
D	VAL382
D	LYS436

site_id	AC5
Number of Residues	4
Details	binding site for residue CA B 801

Chain	Residue
B	GLU242
B	ASP325
B	CYS433
B	ASN436

site_id	AC6
Number of Residues	5
Details	binding site for residue CA B 802

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

site_id	AC7
Number of Residues	6
Details	binding site for residue CA B 803

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

site_id	AC8
Number of Residues	6
Details	binding site for residue CA E 601

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

site_id	AC9
Number of Residues	2
Details	binding site for Mono-Saccharide NAG A 805 bound to ASN A 519

Chain	Residue
A	ASN519
B	ASP566

site_id	AD1
Number of Residues	3
Details	binding site for Mono-Saccharide NAG A 804 bound to ASN A 634

Chain	Residue
A	ILE621
A	SER623
A	ASN634

site_id	AD2
Number of Residues	2
Details	binding site for Mono-Saccharide NAG A 806 bound to ASN A 675

Chain	Residue
A	ASN675
B	ASN233

site_id	AD3
Number of Residues	2
Details	binding site for Mono-Saccharide NAG B 805 bound to ASN B 519

Chain	Residue
A	LYS567
B	ASN519

site_id	AD4
Number of Residues	5
Details	binding site for Mono-Saccharide NAG B 804 bound to ASN B 634

Chain	Residue
B	THR606
B	ILE608
B	LEU625
B	ASN634
B	SER636

site_id	AD5
Number of Residues	2
Details	binding site for Mono-Saccharide NAG B 806 bound to ASN B 675

Chain	Residue
B	SER673
B	ASN675

site_id	AD6
Number of Residues	1
Details	binding site for Mono-Saccharide NAG D 604 bound to ASN D 192

Chain	Residue
D	ASN192

site_id	AD7
Number of Residues	6
Details	binding site for Mono-Saccharide NAG D 602 bound to ASN D 277

Chain	Residue
D	GLN254
D	LYS259
D	ILE261
D	ASN274
D	ASN277
D	ASN428

site_id	AD8
Number of Residues	2
Details	binding site for Mono-Saccharide NAG D 603 bound to ASN D 422

Chain	Residue
D	ASN422
D	HOH703

site_id	AD9
Number of Residues	1
Details	binding site for Mono-Saccharide NAG E 603 bound to ASN E 192

Chain	Residue
E	ASN192

site_id	AE1
Number of Residues	3
Details	binding site for Mono-Saccharide NAG E 602 bound to ASN E 277

Chain	Residue
E	LYS259
E	ASN277
E	ASN428

site_id	AE2
Number of Residues	2
Details	binding site for Mono-Saccharide NAG E 604 bound to ASN E 422

Chain	Residue
A	THR578
E	ASN422

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	398
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	174
Details	Domain: {"description":"Disintegrin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00068","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	74
Details	Domain: {"description":"EGF-like"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
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	42
Details	Repeat: {"description":"LRR 1"}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	42
Details	Repeat: {"description":"LRR 2"}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	42
Details	Repeat: {"description":"LRR 3"}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	100
Details	Domain: {"description":"LRRCT"}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	84
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	84
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	94
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	98
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	86
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	84
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	84
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	6
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)