Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6GBX

Crystal structure of human glutaminyl cyclase variant Y115E-Y117E in complex with SEN177

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0008270	molecular_function	zinc ion binding
A	0016603	molecular_function	glutaminyl-peptide cyclotransferase activity
A	0016740	molecular_function	transferase activity
A	0016746	molecular_function	acyltransferase activity
A	0017186	biological_process	peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase
A	0035580	cellular_component	specific granule lumen
A	0036211	biological_process	protein modification process
A	0046872	molecular_function	metal ion binding
A	0070062	cellular_component	extracellular exosome
A	1904724	cellular_component	tertiary granule lumen
A	1904813	cellular_component	ficolin-1-rich granule lumen
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0008270	molecular_function	zinc ion binding
B	0016603	molecular_function	glutaminyl-peptide cyclotransferase activity
B	0016740	molecular_function	transferase activity
B	0016746	molecular_function	acyltransferase activity
B	0017186	biological_process	peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase
B	0035580	cellular_component	specific granule lumen
B	0036211	biological_process	protein modification process
B	0046872	molecular_function	metal ion binding
B	0070062	cellular_component	extracellular exosome
B	1904724	cellular_component	tertiary granule lumen
B	1904813	cellular_component	ficolin-1-rich granule lumen
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0008270	molecular_function	zinc ion binding
C	0016603	molecular_function	glutaminyl-peptide cyclotransferase activity
C	0016740	molecular_function	transferase activity
C	0016746	molecular_function	acyltransferase activity
C	0017186	biological_process	peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase
C	0035580	cellular_component	specific granule lumen
C	0036211	biological_process	protein modification process
C	0046872	molecular_function	metal ion binding
C	0070062	cellular_component	extracellular exosome
C	1904724	cellular_component	tertiary granule lumen
C	1904813	cellular_component	ficolin-1-rich granule lumen

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN A 401

Chain	Residue
A	ASP159
A	GLU202
A	HIS330
A	S77403

site_id	AC2
Number of Residues	10
Details	binding site for residue SO4 A 402

Chain	Residue
A	HOH539
A	HOH539
A	HOH563
A	HOH575
A	HOH594
A	ARG217
A	ARG312
A	ARG312
A	ARG313
A	HOH513

site_id	AC3
Number of Residues	14
Details	binding site for residue S77 A 403

Chain	Residue
A	LYS144
A	ASP159
A	GLU201
A	GLU202
A	TRP207
A	ASP248
A	GLN304
A	ASP305
A	TRP329
A	HIS330
A	ZN401
A	HOH558
A	HOH581
A	HOH629

site_id	AC4
Number of Residues	8
Details	binding site for residue EDO A 404

Chain	Residue
A	THR126
A	PRO129
A	HIS134
A	GLN194
A	HIS228
A	GLN237
A	HOH501
A	HOH568

site_id	AC5
Number of Residues	3
Details	binding site for residue EDO A 405

Chain	Residue
A	SER323
A	PRO324
A	PHE325

site_id	AC6
Number of Residues	5
Details	binding site for residue EDO A 406

Chain	Residue
A	ASN41
A	ARG266
A	HOH562
A	HOH605
B	HOH585

site_id	AC7
Number of Residues	4
Details	binding site for residue EDO A 407

Chain	Residue
A	ASN128
A	LEU181
A	ASP190
A	LEU191

site_id	AC8
Number of Residues	3
Details	binding site for residue EDO A 408

Chain	Residue
A	HIS239
A	ARG313
A	GLY314

site_id	AC9
Number of Residues	4
Details	binding site for residue ZN B 401

Chain	Residue
B	ASP159
B	GLU202
B	HIS330
B	S77403

site_id	AD1
Number of Residues	10
Details	binding site for residue SO4 B 402

Chain	Residue
B	ARG217
B	ARG312
B	HOH501
B	HOH534
B	HOH596
B	HOH600
B	HOH612
C	ARG312
C	ARG313
C	HOH527

site_id	AD2
Number of Residues	14
Details	binding site for residue S77 B 403

Chain	Residue
B	LYS144
B	ASP159
B	GLU201
B	GLU202
B	TRP207
B	ASP248
B	GLN304
B	ASP305
B	TRP329
B	HIS330
B	ZN401
B	HOH574
B	HOH621
B	HOH629

site_id	AD3
Number of Residues	5
Details	binding site for residue EDO B 404

Chain	Residue
B	LEU238
B	HIS239
B	ARG313
B	GLY314
B	VAL315

site_id	AD4
Number of Residues	6
Details	binding site for residue EDO B 405

Chain	Residue
B	ASN41
B	ASN263
B	ARG266
B	HOH578
B	HOH586
B	HOH633

site_id	AD5
Number of Residues	3
Details	binding site for residue EDO B 406

Chain	Residue
B	ARG270
B	HOH507
C	GLU290

site_id	AD6
Number of Residues	9
Details	binding site for residue EDO B 407

Chain	Residue
B	HOH505
B	HOH506
B	HOH581
B	THR126
B	PRO129
B	HIS134
B	GLN194
B	HIS228
B	GLN237

site_id	AD7
Number of Residues	9
Details	binding site for residue EDO B 408

Chain	Residue
B	ASN41
B	TYR42
B	GLN44
B	ARG266
B	HOH516
B	HOH635
C	ASN254
C	PRO324
C	HOH616

site_id	AD8
Number of Residues	3
Details	binding site for residue EDO B 409

Chain	Residue
B	LEU181
B	ASP190
B	LEU191

site_id	AD9
Number of Residues	4
Details	binding site for residue EDO B 410

Chain	Residue
B	GLN55
C	SER50
C	ARG54
C	HOH510

site_id	AE1
Number of Residues	3
Details	binding site for residue EDO B 411

Chain	Residue
B	SER323
B	PRO324
B	PHE325

site_id	AE2
Number of Residues	4
Details	binding site for residue EDO B 412

Chain	Residue
B	ALA52
B	GLN55
B	LYS177
B	LEU361

site_id	AE3
Number of Residues	4
Details	binding site for residue ZN C 401

Chain	Residue
C	ASP159
C	GLU202
C	HIS330
C	S77403

site_id	AE4
Number of Residues	9
Details	binding site for residue SO4 C 402

Chain	Residue
B	ARG312
B	ARG313
C	ARG217
C	ARG312
C	HOH505
C	HOH508
C	HOH527
C	HOH577
C	HOH599

site_id	AE5
Number of Residues	14
Details	binding site for residue S77 C 403

Chain	Residue
C	LYS144
C	ASP159
C	GLU201
C	GLU202
C	TRP207
C	ASP248
C	GLN304
C	ASP305
C	TRP329
C	HIS330
C	ZN401
C	HOH585
C	HOH588
C	HOH642

site_id	AE6
Number of Residues	5
Details	binding site for residue EDO C 404

Chain	Residue
C	ASN41
C	ARG266
C	HOH565
C	HOH567
C	HOH584

site_id	AE7
Number of Residues	6
Details	binding site for residue EDO C 405

Chain	Residue
B	GLN210
B	HOH509
C	LEU238
C	HIS239
C	ARG313
C	GLY314

site_id	AE8
Number of Residues	4
Details	binding site for residue EDO C 406

Chain	Residue
C	ASN128
C	LEU181
C	ASP190
C	LEU191

site_id	AE9
Number of Residues	3
Details	binding site for residue EDO C 407

Chain	Residue
C	SER323
C	PRO324
C	PHE325

site_id	AF1
Number of Residues	9
Details	binding site for residue EDO C 408

Chain	Residue
C	THR126
C	PRO129
C	HIS134
C	GLN194
C	MET223
C	HIS228
C	GLN237
C	HOH502
C	HOH528

site_id	AF2
Number of Residues	4
Details	binding site for residue EDO C 409

Chain	Residue
C	GLU105
C	ILE124
C	LYS222
C	GLN237

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"18072935","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16135565","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18072935","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21288892","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21671571","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2AFM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2AFO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2AFS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2AFU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2AFW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2AFX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2AFZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZED","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZEE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZEF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZEG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZEH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZEL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZEM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZEN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZEO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZEP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PBB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PBE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SI0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YU9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YWY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	3
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"21671571","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	3
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)