Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5ZE9

Crystal structure of AMP-PNP bound mutant A3B3 complex from Enterococcus hirae V-ATPase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0006811	biological_process	monoatomic ion transport
A	0006814	biological_process	sodium ion transport
A	0035725	biological_process	sodium ion transmembrane transport
A	0042777	biological_process	proton motive force-driven plasma membrane ATP synthesis
A	0045259	cellular_component	proton-transporting ATP synthase complex
A	0046034	biological_process	ATP metabolic process
A	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
A	0046961	molecular_function	proton-transporting ATPase activity, rotational mechanism
A	0046962	molecular_function	sodium-transporting ATPase activity, rotational mechanism
A	1902600	biological_process	proton transmembrane transport
B	0000166	molecular_function	nucleotide binding
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0006811	biological_process	monoatomic ion transport
B	0006814	biological_process	sodium ion transport
B	0035725	biological_process	sodium ion transmembrane transport
B	0042777	biological_process	proton motive force-driven plasma membrane ATP synthesis
B	0045259	cellular_component	proton-transporting ATP synthase complex
B	0046034	biological_process	ATP metabolic process
B	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
B	0046961	molecular_function	proton-transporting ATPase activity, rotational mechanism
B	0046962	molecular_function	sodium-transporting ATPase activity, rotational mechanism
B	1902600	biological_process	proton transmembrane transport
C	0000166	molecular_function	nucleotide binding
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0006811	biological_process	monoatomic ion transport
C	0006814	biological_process	sodium ion transport
C	0035725	biological_process	sodium ion transmembrane transport
C	0042777	biological_process	proton motive force-driven plasma membrane ATP synthesis
C	0045259	cellular_component	proton-transporting ATP synthase complex
C	0046034	biological_process	ATP metabolic process
C	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
C	0046961	molecular_function	proton-transporting ATPase activity, rotational mechanism
C	0046962	molecular_function	sodium-transporting ATPase activity, rotational mechanism
C	1902600	biological_process	proton transmembrane transport
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0006811	biological_process	monoatomic ion transport
D	0006814	biological_process	sodium ion transport
D	0042777	biological_process	proton motive force-driven plasma membrane ATP synthesis
D	0046034	biological_process	ATP metabolic process
D	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
D	1902600	biological_process	proton transmembrane transport
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0006811	biological_process	monoatomic ion transport
E	0006814	biological_process	sodium ion transport
E	0042777	biological_process	proton motive force-driven plasma membrane ATP synthesis
E	0046034	biological_process	ATP metabolic process
E	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
E	1902600	biological_process	proton transmembrane transport
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0006811	biological_process	monoatomic ion transport
F	0006814	biological_process	sodium ion transport
F	0042777	biological_process	proton motive force-driven plasma membrane ATP synthesis
F	0046034	biological_process	ATP metabolic process
F	0046933	molecular_function	proton-transporting ATP synthase activity, rotational mechanism
F	1902600	biological_process	proton transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	25
Details	binding site for residue ANP A 601

Chain	Residue
A	PHE234
A	PHE425
A	ASN504
A	ALA505
A	PHE506
A	MG602
A	GOL605
A	HOH704
A	HOH711
A	HOH765
A	HOH766
A	GLY235
A	HOH783
A	HOH786
A	HOH809
A	HOH816
D	TYR321
D	ARG350
A	ALA236
A	GLY237
A	LYS238
A	THR239
A	VAL240
A	GLU261
A	ARG262

site_id	AC2
Number of Residues	5
Details	binding site for residue MG A 602

Chain	Residue
A	THR239
A	ANP601
A	HOH704
A	HOH765
A	HOH783

site_id	AC3
Number of Residues	7
Details	binding site for residue GOL A 603

Chain	Residue
A	GLN50
A	ARG194
A	GLU304
A	MET341
A	TYR357
A	ARG361
A	HOH759

site_id	AC4
Number of Residues	8
Details	binding site for residue GOL A 604

Chain	Residue
A	TYR357
A	ARG361
A	HOH706
A	HOH747
A	HOH806
A	HOH845
E	GLY13
E	HOH706

site_id	AC5
Number of Residues	4
Details	binding site for residue GOL A 605

Chain	Residue
A	ANP601
A	GOL607
A	HOH718
D	ARG350

site_id	AC6
Number of Residues	4
Details	binding site for residue GOL A 606

Chain	Residue
A	LEU419
A	ASN429
A	TRP430
A	ILE431

site_id	AC7
Number of Residues	6
Details	binding site for residue GOL A 607

Chain	Residue
A	HIS243
A	GLN244
A	LYS247
A	ALA505
A	PHE506
A	GOL605

site_id	AC8
Number of Residues	8
Details	binding site for residue GOL A 608

Chain	Residue
A	ARG423
A	HOH716
A	HOH819
D	LEU138
D	ASN139
D	ASN370
D	PHE373
D	HOH619

site_id	AC9
Number of Residues	3
Details	binding site for residue GOL A 609

Chain	Residue
A	PHE102
A	HOH701
A	HOH713

site_id	AD1
Number of Residues	25
Details	binding site for residue ANP B 601

Chain	Residue
B	GLY235
B	ALA236
B	GLY237
B	LYS238
B	THR239
B	VAL240
B	GLU261
B	ARG262
B	PHE425
B	ASN504
B	ALA505
B	PHE506
B	MG602
B	GOL610
B	HOH704
B	HOH731
B	HOH733
B	HOH746
B	HOH795
B	HOH834
B	HOH853
B	HOH921
E	TYR321
E	ARG350
E	LYS352

site_id	AD2
Number of Residues	5
Details	binding site for residue MG B 602

Chain	Residue
B	HOH795
B	THR239
B	ANP601
B	HOH731
B	HOH746

site_id	AD3
Number of Residues	6
Details	binding site for residue GOL B 603

Chain	Residue
B	ASP416
B	SER418
B	LEU419
B	ASN429
B	TRP430
B	GLU468

site_id	AD4
Number of Residues	6
Details	binding site for residue GOL B 604

Chain	Residue
B	GLN432
B	HOH705
B	HOH843
B	HOH855
F	ARG331
F	LYS335

site_id	AD5
Number of Residues	7
Details	binding site for residue GOL B 605

Chain	Residue
B	HIS243
B	GLN244
B	LYS247
B	ALA505
B	PHE506
B	GOL610
B	HOH814

site_id	AD6
Number of Residues	2
Details	binding site for residue GOL B 606

Chain	Residue
B	ASN153
B	ARG195

site_id	AD7
Number of Residues	4
Details	binding site for residue GOL B 607

Chain	Residue
B	GLY414
B	LEU415
B	ASP416
B	ASN429

site_id	AD8
Number of Residues	7
Details	binding site for residue GOL B 608

Chain	Residue
B	PHE234
B	SER417
B	HOH702
B	HOH836
E	GLN326
E	LEU348
E	HOH632

site_id	AD9
Number of Residues	7
Details	binding site for residue GOL B 609

Chain	Residue
B	GLU41
B	GLU347
B	TYR357
B	ARG361
B	HOH724
B	HOH748
B	HOH820

site_id	AE1
Number of Residues	6
Details	binding site for residue GOL B 610

Chain	Residue
B	VAL240
B	PHE506
B	ANP601
B	GOL605
B	HOH703
E	ARG350

site_id	AE2
Number of Residues	6
Details	binding site for residue GOL B 611

Chain	Residue
B	VAL270
B	ASN271
B	GLU275
E	LYS3
E	GLU4
E	TYR5

site_id	AE3
Number of Residues	4
Details	binding site for residue GOL B 612

Chain	Residue
B	MET95
B	GLN99
B	SER100
B	ASN101

site_id	AE4
Number of Residues	27
Details	binding site for residue ANP C 601

Chain	Residue
C	PHE234
C	GLY235
C	ALA236
C	GLY237
C	LYS238
C	THR239
C	VAL240
C	GLU261
C	ARG262
C	PHE425
C	ASN504
C	ALA505
C	PHE506
C	MG602
C	HOH702
C	HOH708
C	HOH737
C	HOH750
C	HOH764
C	HOH787
C	HOH832
F	GLY320
F	TYR321
F	ARG350
F	LYS352
F	GOL507
F	HOH701

site_id	AE5
Number of Residues	5
Details	binding site for residue MG C 602

Chain	Residue
C	THR239
C	ANP601
C	HOH737
C	HOH750
C	HOH764

site_id	AE6
Number of Residues	5
Details	binding site for residue GOL C 603

Chain	Residue
C	GLY414
C	LEU415
C	ASP416
C	ASN429
C	HOH728

site_id	AE7
Number of Residues	6
Details	binding site for residue GOL C 604

Chain	Residue
C	ASP416
C	SER418
C	LEU419
C	ASN429
C	TRP430
C	ILE431

site_id	AE8
Number of Residues	6
Details	binding site for residue GOL C 606

Chain	Residue
C	GLU54
C	HOH719
F	GLU27
F	ARG226
F	THR283
F	GOL501

site_id	AE9
Number of Residues	5
Details	binding site for residue GOL C 607

Chain	Residue
C	ILE397
C	GLN403
C	LEU406
C	HOH717
C	HOH847

site_id	AF1
Number of Residues	4
Details	binding site for residue GOL C 608

Chain	Residue
C	HIS243
C	GLN244
C	LYS247
F	GOL507

site_id	AF2
Number of Residues	5
Details	binding site for residue GOL C 609

Chain	Residue
C	SER81
C	GLN82
C	MET83
C	ASP92
C	VAL270

site_id	AF3
Number of Residues	6
Details	binding site for residue GOL C 610

Chain	Residue
C	TRP248
C	LEU276
C	ASP278
C	GLU283
C	LEU285
C	HOH908

site_id	AF4
Number of Residues	9
Details	binding site for residue MES D 501

Chain	Residue
C	MET95
C	GLU96
C	GLN99
C	SER100
C	ASN101
D	TYR418
D	HOH647
F	ARG292
F	GLY293

site_id	AF5
Number of Residues	5
Details	binding site for residue GOL D 502

Chain	Residue
C	GLU96
C	VAL97
D	GLN339
D	ASN414
D	GLY416

site_id	AF6
Number of Residues	4
Details	binding site for residue GOL D 503

Chain	Residue
A	ASN297
D	ASN112
D	GLY113
D	THR283

site_id	AF7
Number of Residues	4
Details	binding site for residue GOL D 504

Chain	Residue
D	GLN371
D	GLU441
D	LYS443
D	ARG444

site_id	AF8
Number of Residues	6
Details	binding site for residue GOL E 501

Chain	Residue
B	ASN297
E	ASN112
E	GLY113
E	GLU114
E	THR283
E	ARG287

site_id	AF9
Number of Residues	5
Details	binding site for residue GOL E 502

Chain	Residue
B	PHE102
E	TYR234
E	GLU238
E	HOH628
E	HOH641

site_id	AG1
Number of Residues	6
Details	binding site for residue GOL E 503

Chain	Residue
E	GLN78
E	LEU79
E	GLY80
E	LEU93
E	TYR108
E	HOH719

site_id	AG2
Number of Residues	4
Details	binding site for residue GOL E 504

Chain	Residue
A	HOH748
A	HOH788
E	ARG331
E	HOH601

site_id	AG3
Number of Residues	6
Details	binding site for residue GOL F 501

Chain	Residue
C	GLU54
C	ASN297
C	GOL606
F	ASN112
F	THR283
F	ARG287

site_id	AG4
Number of Residues	1
Details	binding site for residue GOL F 502

Chain	Residue
F	THR361

site_id	AG5
Number of Residues	5
Details	binding site for residue GOL F 503

Chain	Residue
C	GLN447
F	GLY80
F	GLY94
F	ILE103
F	HOH616

site_id	AG6
Number of Residues	3
Details	binding site for residue GOL F 504

Chain	Residue
F	ASP176
F	ARG206
F	MET241

site_id	AG7
Number of Residues	3
Details	binding site for residue GOL F 505

Chain	Residue
D	GLN200
F	TYR237
F	HOH693

site_id	AG8
Number of Residues	4
Details	binding site for residue GOL F 506

Chain	Residue
F	ARG264
F	ARG265
F	HOH646
F	HOH681

site_id	AG9
Number of Residues	7
Details	binding site for residue GOL F 507

Chain	Residue
C	THR239
C	PHE506
C	ANP601
C	GOL608
C	HOH831
C	HOH867
F	ARG350

Functional Information from PROSITE/UniProt

site_id	PS00152
Number of Residues	10
Details	ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PSINWIQSYS

Chain	Residue	Details
A	PRO426-SER435
D	PRO340-SER349

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	21
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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