1N5D

CRYSTAL STRUCTURE OF PORCINE TESTICULAR CARBONYL REDUCTASE/ 20BETA-HYDROXYSTEROID DEHYDROGENASE

Replaces:  1HU4

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004090	molecular_function	carbonyl reductase (NADPH) activity
A	0005737	cellular_component	cytoplasm
A	0006629	biological_process	lipid metabolic process
A	0006805	biological_process	xenobiotic metabolic process
A	0008106	molecular_function	alcohol dehydrogenase (NADP+) activity
A	0016491	molecular_function	oxidoreductase activity
A	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0018455	molecular_function	alcohol dehydrogenase [NAD(P)+] activity
A	0042373	biological_process	vitamin K metabolic process
A	0047020	molecular_function	15-hydroxyprostaglandin-D dehydrogenase (NADP+) activity
A	0047021	molecular_function	15-hydroxyprostaglandin dehydrogenase (NADP+) activity
A	0050221	molecular_function	prostaglandin E2 9-reductase activity
A	0160163	molecular_function	S-nitrosoglutathione reductase (NADPH) activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 400

Chain	Residue
A	ARG57
A	PHE58

---

site_id	AC2
Number of Residues	32
Details	BINDING SITE FOR RESIDUE NDP A 300

Chain	Residue
A	LEU61
A	ASP62
A	ILE63
A	ILE64
A	ASN89
A	ALA90
A	ALA91
A	ILE92
A	ASP97
A	VAL137
A	SER138
A	SER139
A	TYR193
A	LYS197
A	PRO227
A	GLY228
A	TRP229
A	VAL230
A	THR232
A	MET234
A	GLY11
A	GLY235
A	HOH401
A	HOH405
A	HOH411
A	HOH413
A	ASN13
A	LYS14
A	GLY15
A	ILE16
A	ARG37
A	ARG41

---

Functional Information from PROSITE/UniProt

site_id	PS00061
Number of Residues	29
Details	ADH_SHORT Short-chain dehydrogenases/reductases family signature. NgvhrkegwsDstYGVTKIGVsVLSrIYA

Chain	Residue	Details
A	ASN180-ALA208

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10001","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11279087","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	13
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P16152","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P47727","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"N6-1-carboxyethyl lysine","evidences":[{"source":"UniProtKB","id":"P16152","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1db3

Chain	Residue	Details
A	TYR193
A	SER139
A	GLU141
A	LYS197

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1db3

Chain	Residue	Details
A	ASN113
A	TYR193
A	SER139
A	LYS197

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1db3

Chain	Residue	Details
A	LYS197
A	TRP188

---

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1db3

Chain	Residue	Details
A	TYR193
A	LYS197

---