Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5BPK

Varying binding modes of inhibitors and structural differences in the binding pockets of different gamma-glutamyltranspeptidases

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006751	biological_process	glutathione catabolic process
A	0036374	molecular_function	glutathione hydrolase activity
B	0006751	biological_process	glutathione catabolic process
B	0036374	molecular_function	glutathione hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	binding site for residue EDO A 401

Chain	Residue
A	TYR29
D	HOH815

site_id	AC2
Number of Residues	5
Details	binding site for residue EDO A 402

Chain	Residue
A	HIS76
A	HOH534
A	HOH611
C	LYS565
C	HOH809

site_id	AC3
Number of Residues	7
Details	binding site for residue EDO A 403

Chain	Residue
A	PHE197
A	PHE198
A	ASP204
A	TYR205
A	HOH647
A	LEU180
A	ARG184

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

Chain	Residue
A	SER28
A	TYR29
B	SER28
B	TYR29
C	SER499
C	HOH802
D	SER499
D	HOH801

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

Chain	Residue
A	ASP341
A	ASN345
A	HOH694

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

Chain	Residue
A	ARG272
A	GLY273
A	TYR274
C	LYS460
C	ASN461

site_id	AC7
Number of Residues	2
Details	binding site for residue EDO A 407

Chain	Residue
A	GLU297
A	HOH744

site_id	AC8
Number of Residues	5
Details	binding site for residue EDO A 408

Chain	Residue
A	ASN94
A	LEU188
A	LYS189
A	SER191
A	LYS194

site_id	AC9
Number of Residues	4
Details	binding site for residue EDO A 409

Chain	Residue
A	ALA145
A	LYS148
A	LYS149
A	TRP263

site_id	AD1
Number of Residues	4
Details	binding site for residue EDO A 410

Chain	Residue
A	ASN260
A	HOH621
B	LYS253
B	ALA257

site_id	AD2
Number of Residues	14
Details	binding site for residue 4UD C 701

Chain	Residue
A	ARG103
C	THR380
C	THR398
C	ASN400
C	GLU419
C	ASP422
C	TYR433
C	SER451
C	SER452
C	MET453
C	GLY472
C	GLY473
C	ILE476
C	HOH835

site_id	AD3
Number of Residues	9
Details	binding site for residue EDO C 702

Chain	Residue
A	HIS91
A	ALA93
A	HOH511
C	GLY390
C	ASN462
C	LYS463
C	VAL464
C	EDO707
C	HOH816

site_id	AD4
Number of Residues	10
Details	binding site for residue EDO C 703

Chain	Residue
A	ARG326
C	ASP422
C	PHE423
C	SER424
C	ASN429
C	ASN431
C	LEU435
C	ASN441
C	HOH849
C	HOH868

site_id	AD5
Number of Residues	8
Details	binding site for residue EDO C 704

Chain	Residue
C	PRO501
C	ARG502
C	PHE503
C	ILE514
C	GLU515
C	GLY518
C	HOH807
C	HOH875

site_id	AD6
Number of Residues	7
Details	binding site for residue EDO C 705

Chain	Residue
A	PRO30
B	TYR29
C	SER495
C	SER560
C	THR561
C	HOH802
C	HOH837

site_id	AD7
Number of Residues	7
Details	binding site for residue EDO C 706

Chain	Residue
C	HOH867
A	ALA93
A	LYS194
A	HIS202
C	ASN391
C	EDO711
C	HOH820

site_id	AD8
Number of Residues	6
Details	binding site for residue EDO C 707

Chain	Residue
C	ASP387
C	GLY390
C	SER555
C	EDO702
C	HOH839
C	HOH861

site_id	AD9
Number of Residues	6
Details	binding site for residue EDO C 708

Chain	Residue
A	MET296
A	ASN311
C	SER485
C	TYR490
C	HOH823
C	HOH836

site_id	AE1
Number of Residues	5
Details	binding site for residue EDO C 709

Chain	Residue
C	LYS516
C	PRO538
C	VAL539
C	HOH862
C	HOH883

site_id	AE2
Number of Residues	6
Details	binding site for residue EDO C 710

Chain	Residue
C	ASP522
C	ASP525
C	ASN526
C	HOH817
C	HOH841
D	ASN526

site_id	AE3
Number of Residues	7
Details	binding site for residue EDO C 711

Chain	Residue
A	THR152
A	GLY201
A	HIS202
C	TRP389
C	EDO706
C	HOH804
C	HOH820

site_id	AE4
Number of Residues	3
Details	binding site for residue EDO B 401

Chain	Residue
B	GLU167
B	LYS214
B	HOH565

site_id	AE5
Number of Residues	6
Details	binding site for residue EDO B 402

Chain	Residue
B	THR152
B	GLY201
B	HIS202
B	HOH574
B	HOH711
D	TRP389

site_id	AE6
Number of Residues	6
Details	binding site for residue EDO B 403

Chain	Residue
B	LYS194
B	HIS202
B	HOH711
D	TRP389
D	ASN391
D	HOH879

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

Chain	Residue
B	SER42
B	SER43
B	HIS44
B	PRO45
B	SER48
D	LYS565

site_id	AE8
Number of Residues	6
Details	binding site for residue EDO B 406

Chain	Residue
B	ASN94
B	LEU188
B	LYS189
B	SER191
B	LYS194
B	HOH778

site_id	AE9
Number of Residues	4
Details	binding site for residue EDO B 407

Chain	Residue
B	LYS199
B	ASP204
B	GLN206
B	EDO412

site_id	AF1
Number of Residues	5
Details	binding site for residue EDO B 408

Chain	Residue
B	PHE353
B	ILE356
B	GLN357
B	PRO358
B	HOH616

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

Chain	Residue
B	LYS262
B	ASP334
C	GLU444
C	HOH944

site_id	AF3
Number of Residues	4
Details	binding site for residue EDO B 410

Chain	Residue
B	LYS109
B	GLU241
B	LYS245
B	HOH682

site_id	AF4
Number of Residues	4
Details	binding site for residue EDO B 411

Chain	Residue
B	LYS33
B	ASN34
B	GLN52
B	HOH519

site_id	AF5
Number of Residues	4
Details	binding site for residue EDO B 412

Chain	Residue
B	LEU203
B	ASP204
B	EDO407
D	ARG388

site_id	AF6
Number of Residues	6
Details	binding site for residue EDO B 413

Chain	Residue
B	LEU180
B	ARG184
B	PHE197
B	PHE198
B	ASP204
B	TYR205

site_id	AF7
Number of Residues	8
Details	binding site for residue EDO D 702

Chain	Residue
A	ALA27
A	HOH597
B	ALA27
C	SER499
D	SER499
D	HOH806
D	HOH854
D	HOH864

site_id	AF8
Number of Residues	3
Details	binding site for residue EDO D 703

Chain	Residue
D	ASP510
D	GLU511
D	GLN533

site_id	AF9
Number of Residues	5
Details	binding site for residue EDO D 704

Chain	Residue
A	LEU304
D	ALA521
D	ASP525
D	HOH880
D	HOH917

site_id	AG1
Number of Residues	8
Details	binding site for residue EDO D 705

Chain	Residue
D	PRO501
D	ARG502
D	PHE503
D	ILE514
D	GLU515
D	GLY518
D	HOH814
D	HOH856

site_id	AG2
Number of Residues	8
Details	binding site for residue EDO D 706

Chain	Residue
A	TYR29
B	PRO30
B	ILE32
D	SER495
D	SER560
D	THR561
D	HOH801
D	HOH815

site_id	AG3
Number of Residues	5
Details	binding site for residue EDO D 707

Chain	Residue
B	ASN311
D	SER485
D	TYR490
D	HOH807
D	HOH846

site_id	AG4
Number of Residues	10
Details	binding site for residue EDO D 708

Chain	Residue
B	ARG326
D	ASP422
D	PHE423
D	ASN429
D	ASN431
D	LEU435
D	ASN441
D	HOH850
D	HOH862
D	HOH911

site_id	AG5
Number of Residues	9
Details	binding site for residue EDO D 709

Chain	Residue
D	ASP387
D	ARG388
D	TRP389
D	GLY390
D	SER555
D	PHE557
D	HOH852
D	HOH873
D	HOH897

site_id	AG6
Number of Residues	5
Details	binding site for residue EDO D 710

Chain	Residue
C	ASN526
C	HOH841
D	ASP522
D	ASP525
D	HOH818

site_id	AG7
Number of Residues	2
Details	binding site for residue EDO D 711

Chain	Residue
D	ARG475
D	ARG513

site_id	AG8
Number of Residues	20
Details	binding site for Di-peptide 4UD D 701 and THR D 380

Chain	Residue
B	ALA79
B	ARG103
D	THR381
D	TYR397
D	THR398
D	ASN400
D	GLU419
D	ASP422
D	TYR433
D	SER451
D	SER452
D	MET453
D	PRO471
D	GLY472
D	GLY473
D	ILE476
D	HOH855
D	HOH857
D	HOH860
D	HOH914

site_id	AG9
Number of Residues	20
Details	binding site for Di-peptide 4UD D 701 and THR D 380

Chain	Residue
B	ALA79
B	ARG103
D	THR381
D	TYR397
D	THR398
D	ASN400
D	GLU419
D	ASP422
D	TYR433
D	SER451
D	SER452
D	MET453
D	PRO471
D	GLY472
D	GLY473
D	ILE476
D	HOH855
D	HOH857
D	HOH860
D	HOH914

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	28
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGGGGFAVIHlAngenvaldfrek......APLK

Chain	Residue	Details
A	ILE82-LYS109

site_id	PS00462
Number of Residues	25
Details	G_GLU_TRANSPEPTIDASE Gamma-glutamyltranspeptidase signature. TTHySVadrwGNaVSvTyTINasYG

Chain	Residue	Details
C	THR380-GLY404

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