2XDW

Inhibition of Prolyl Oligopeptidase with a Synthetic Unnatural Dipeptide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004252	molecular_function	serine-type endopeptidase activity
A	0005737	cellular_component	cytoplasm
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0008236	molecular_function	serine-type peptidase activity
A	0016787	molecular_function	hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE TAM A 1711

Chain	Residue
A	ILE118
A	HOH2308
A	HOH2868
A	HOH3041
A	HOH3042
A	HOH3043
A	LEU119
A	SER120
A	ASP121
A	LYS445
A	ASP446
A	ASN522
A	ASN525
A	HOH2123

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 1712

Chain	Residue
A	LYS48
A	ARG312
A	GLU323
A	TRP326
A	VAL328
A	HOH2668
A	HOH3044

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 1713

Chain	Residue
A	ALA226
A	GLU227
A	PHE228
A	ILE276
A	LYS281
A	HOH3045
A	HOH3046
A	HOH3047

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 1714

Chain	Residue
A	GLY553
A	SER554
A	VAL578
A	HIS680
A	HOH3048

---

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL A 1715

Chain	Residue
A	PRO568
A	ASP569
A	PHE571
A	GLY572
A	ILE628
A	GLN629
A	PRO631
A	ASN668
A	HOH3050
A	HOH3051

---

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 1716

Chain	Residue
A	GLU239
A	ASP291
A	TYR292
A	HOH2555
A	HOH3053
A	HOH3054
A	HOH3055
A	HOH3056
A	HOH3057

---

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 1717

Chain	Residue
A	VAL341
A	HOH2633
A	HOH3054
A	HOH3055
A	HOH3058
A	HOH3059

---

site_id	AC8
Number of Residues	12
Details	BINDING SITE FOR RESIDUE GOL A 1718

Chain	Residue
A	PRO7
A	ASP8
A	VAL9
A	TRP30
A	GLN38
A	ALA41
A	PHE42
A	HOH2435
A	HOH3060
A	HOH3061
A	HOH3062
A	HOH3063

---

site_id	AC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 1719

Chain	Residue
A	GLU287
A	ASN305
A	GLU512
A	LYS516
A	HOH2646
A	HOH2855
A	HOH3064
A	HOH3065

---

site_id	BC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 1720

Chain	Residue
A	TYR190
A	PRO191
A	GLN193
A	THR204
A	ASN205
A	LEU206
A	HOH2459
A	HOH3068

---

Functional Information from PROSITE/UniProt

site_id	PS00708
Number of Residues	31
Details	PRO_ENDOPEP_SER Prolyl endopeptidase family serine active site. DfqcAaeyLikegytspkrltinGgSnGGLL

Chain	Residue	Details
A	ASP529-LEU559

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU10084","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1900195","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Charge relay system"}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU10084","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"2064618","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"UniProtKB","id":"P48147","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P48147","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 901

Chain	Residue	Details
A	TYR473	electrostatic stabiliser
A	SER554	covalent catalysis, proton shuttle (general acid/base)
A	ASP641	electrostatic stabiliser, modifies pKa
A	HIS680	proton shuttle (general acid/base)

---