Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6FPC

Structure of the PRO-PRO endopeptidase (PPEP-2) from Paenibacillus alvei

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0008237	molecular_function	metallopeptidase activity
A	0016787	molecular_function	hydrolase activity
A	0046872	molecular_function	metal ion binding
B	0005576	cellular_component	extracellular region
B	0006508	biological_process	proteolysis
B	0008233	molecular_function	peptidase activity
B	0008237	molecular_function	metallopeptidase activity
B	0016787	molecular_function	hydrolase activity
B	0046872	molecular_function	metal ion binding
C	0005576	cellular_component	extracellular region
C	0006508	biological_process	proteolysis
C	0008233	molecular_function	peptidase activity
C	0008237	molecular_function	metallopeptidase activity
C	0016787	molecular_function	hydrolase activity
C	0046872	molecular_function	metal ion binding
D	0005576	cellular_component	extracellular region
D	0006508	biological_process	proteolysis
D	0008233	molecular_function	peptidase activity
D	0008237	molecular_function	metallopeptidase activity
D	0016787	molecular_function	hydrolase activity
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue ZN A 301

Chain	Residue
A	HIS137
A	HIS141
A	TYR174
A	GLU181
A	HOH495

site_id	AC2
Number of Residues	5
Details	binding site for residue CD A 302

Chain	Residue
A	HOH495
A	HIS137
A	HIS141
A	TYR174
A	GLU181

site_id	AC3
Number of Residues	4
Details	binding site for residue CD A 303

Chain	Residue
A	HIS46
A	HOH514
A	HOH525
C	HOH489

site_id	AC4
Number of Residues	3
Details	binding site for residue CD A 304

Chain	Residue
A	GLU43
A	HIS46
A	HOH419

site_id	AC5
Number of Residues	5
Details	binding site for residue ZN B 301

Chain	Residue
B	HIS137
B	HIS141
B	TYR174
B	GLU181
C	HOH501

site_id	AC6
Number of Residues	5
Details	binding site for residue CD B 302

Chain	Residue
B	HIS137
B	HIS141
B	TYR174
B	GLU181
C	HOH501

site_id	AC7
Number of Residues	3
Details	binding site for residue CD B 303

Chain	Residue
B	HIS46
C	LYS213
C	ALA216

site_id	AC8
Number of Residues	2
Details	binding site for residue CD B 304

Chain	Residue
B	ASP194
D	HOH510

site_id	AC9
Number of Residues	4
Details	binding site for residue SO4 B 305

Chain	Residue
B	TYR44
B	ASN45
B	HIS46
B	SER47

site_id	AD1
Number of Residues	4
Details	binding site for residue SO4 B 306

Chain	Residue
B	ARG119
B	HOH442
B	HOH457
B	HOH488

site_id	AD2
Number of Residues	5
Details	binding site for residue SO4 B 307

Chain	Residue
B	PRO40
B	SER41
B	GLY42
B	HOH433
B	HOH435

site_id	AD3
Number of Residues	2
Details	binding site for residue SO4 B 308

Chain	Residue
B	GLY42
B	GLU43

site_id	AD4
Number of Residues	5
Details	binding site for residue ZN C 301

Chain	Residue
C	HIS137
C	HIS141
C	TYR174
C	GLU181
C	HOH453

site_id	AD5
Number of Residues	5
Details	binding site for residue CD C 302

Chain	Residue
C	HIS137
C	HIS141
C	TYR174
C	GLU181
C	HOH453

site_id	AD6
Number of Residues	4
Details	binding site for residue CD C 303

Chain	Residue
C	GLU29
C	GLN54
C	GLU57
C	HOH474

site_id	AD7
Number of Residues	1
Details	binding site for residue CD C 304

Chain	Residue
C	HIS46

site_id	AD8
Number of Residues	3
Details	binding site for residue CD C 305

Chain	Residue
C	HIS46
C	HOH419
C	HOH503

site_id	AD9
Number of Residues	5
Details	binding site for residue SO4 C 306

Chain	Residue
B	ARG96
C	TYR89
C	TYR122
C	HOH427
C	HOH428

site_id	AE1
Number of Residues	7
Details	binding site for residue SO4 C 307

Chain	Residue
C	TYR44
C	ASN45
C	HIS46
C	SER47
C	HOH410
C	HOH423
C	HOH468

site_id	AE2
Number of Residues	7
Details	binding site for residue SO4 C 308

Chain	Residue
B	HOH420
C	PRO40
C	SER41
C	LYS75
C	THR77
C	HOH424
C	HOH482

site_id	AE3
Number of Residues	4
Details	binding site for residue SO4 C 309

Chain	Residue
C	SER193
C	ASP194
C	SO4311
C	HOH457

site_id	AE4
Number of Residues	3
Details	binding site for residue SO4 C 310

Chain	Residue
C	THR154
C	ASP155
C	HOH444

site_id	AE5
Number of Residues	6
Details	binding site for residue SO4 C 311

Chain	Residue
C	LYS58
C	SO4309
C	HOH421
C	HOH449
D	SER198
D	HOH402

site_id	AE6
Number of Residues	3
Details	binding site for residue SO4 C 312

Chain	Residue
C	HOH422
C	PRO60
C	THR61

site_id	AE7
Number of Residues	4
Details	binding site for residue ZN D 301

Chain	Residue
D	HIS137
D	HIS141
D	GLU181
D	HOH427

site_id	AE8
Number of Residues	4
Details	binding site for residue CD D 302

Chain	Residue
D	HIS137
D	HIS141
D	GLU181
D	HOH427

site_id	AE9
Number of Residues	4
Details	binding site for residue CD D 303

Chain	Residue
B	HOH491
D	ASP155
D	SO4306
D	HOH493

site_id	AF1
Number of Residues	4
Details	binding site for residue CD D 304

Chain	Residue
D	HIS46
D	GLU156
D	SO4306
D	HOH516

site_id	AF2
Number of Residues	5
Details	binding site for residue CD D 305

Chain	Residue
C	ASP107
C	HOH518
D	GLU43
D	ASN159
D	HOH488

site_id	AF3
Number of Residues	8
Details	binding site for residue SO4 D 306

Chain	Residue
D	HIS46
D	THR154
D	ASP155
D	GLU156
D	CD303
D	CD304
D	HOH406
D	HOH493

site_id	AF4
Number of Residues	6
Details	binding site for residue SO4 D 307

Chain	Residue
A	ARG96
D	TYR89
D	TYR122
D	LYS127
D	HOH401
D	HOH469

site_id	AF5
Number of Residues	7
Details	binding site for residue SO4 D 308

Chain	Residue
A	GLY171
A	ASP172
A	HOH409
D	SER41
D	LYS75
D	THR77
D	HOH497

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255\|PROSITE-ProRule:PRU01339

Chain	Residue	Details
A	GLU138
B	GLU138
C	GLU138
D	GLU138

site_id	SWS_FT_FI2
Number of Residues	16
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU01339, ECO:0000269\|PubMed:29794027

Chain	Residue	Details
A	HIS137
C	HIS141
C	TYR174
C	GLU181
D	HIS137
D	HIS141
D	TYR174
D	GLU181
A	HIS141
A	TYR174
A	GLU181
B	HIS137
B	HIS141
B	TYR174
B	GLU181
C	HIS137

site_id	SWS_FT_FI3
Number of Residues	4
Details	SITE: Transition state stabilizer => ECO:0000250\|UniProtKB:Q183R7

Chain	Residue	Details
A	TYR174
B	TYR174
C	TYR174
D	TYR174

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