1SM9

Crystal Structure Of An Engineered K274RN276D Double Mutant of Xylose Reductase From Candida Tenuis Optimized To Utilize NAD

Functional Information from GO Data

Chain	GOid	namespace	contents
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	0032866	molecular_function	D-xylose reductase (NADPH) activity
A	0042732	biological_process	D-xylose metabolic process
A	0042843	biological_process	D-xylose catabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B	0032866	molecular_function	D-xylose reductase (NADPH) activity
B	0042732	biological_process	D-xylose metabolic process
B	0042843	biological_process	D-xylose catabolic process
C	0016491	molecular_function	oxidoreductase activity
C	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C	0032866	molecular_function	D-xylose reductase (NADPH) activity
C	0042732	biological_process	D-xylose metabolic process
C	0042843	biological_process	D-xylose catabolic process
D	0016491	molecular_function	oxidoreductase activity
D	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D	0032866	molecular_function	D-xylose reductase (NADPH) activity
D	0042732	biological_process	D-xylose metabolic process
D	0042843	biological_process	D-xylose catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	28
Details	BINDING SITE FOR RESIDUE NAD A 1350

Chain	Residue
A	GLY22
A	GLN191
A	TYR217
A	SER218
A	PHE220
A	GLN223
A	SER224
A	GLU227
A	PHE240
A	ALA257
A	ILE272
A	CYS23
A	PRO273
A	ARG274
A	ASP276
A	ARG280
A	ASN284
A	ASN310
A	HOH1369
A	HOH1405
A	HOH1456
A	TRP24
A	ASP47
A	TYR52
A	LYS81
A	HIS114
A	SER169
A	ASN170

---

site_id	AC2
Number of Residues	33
Details	BINDING SITE FOR RESIDUE NAD B 2350

Chain	Residue
B	GLY22
B	CYS23
B	TRP24
B	ASP47
B	TYR52
B	LYS81
B	HIS114
B	SER169
B	ASN170
B	GLN191
B	TYR217
B	SER218
B	SER219
B	PHE220
B	GLN223
B	SER224
B	GLU227
B	ASN229
B	PHE240
B	ALA257
B	ILE272
B	PRO273
B	ARG274
B	ASP276
B	ARG280
B	ASN284
B	ASN310
B	HOH2359
B	HOH2376
B	HOH2417
B	HOH2421
B	HOH2424
B	HOH2431

---

site_id	AC3
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NAD C 3350

Chain	Residue
C	GLY22
C	CYS23
C	TRP24
C	LYS25
C	ASP47
C	TYR52
C	LYS81
C	HIS114
C	SER169
C	ASN170
C	GLN191
C	TYR217
C	SER218
C	PHE220
C	GLN223
C	SER224
C	GLU227
C	ALA257
C	ILE272
C	PRO273
C	ARG274
C	ASP276
C	ARG280
C	ASN284
C	ASN310
C	HOH3364
C	HOH3386
C	HOH3411
C	HOH3502
C	HOH3530

---

site_id	AC4
Number of Residues	32
Details	BINDING SITE FOR RESIDUE NAD D 4350

Chain	Residue
D	GLN191
D	TYR217
D	SER218
D	SER219
D	PHE220
D	GLN223
D	SER224
D	GLU227
D	ASN229
D	PHE240
D	ALA257
D	ILE272
D	PRO273
D	ARG274
D	ASP276
D	ARG280
D	ASN284
D	ASN310
D	HOH4368
D	HOH4380
D	HOH4412
D	HOH4443
D	HOH4446
D	HOH4454
D	GLY22
D	CYS23
D	TRP24
D	ASP47
D	TYR52
D	LYS81
D	SER169
D	ASN170

---

Functional Information from PROSITE/UniProt

site_id	PS00062
Number of Residues	18
Details	ALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. LeklvaagkIKSIGVSNF

Chain	Residue	Details
A	LEU154-PHE171

---

site_id	PS00063
Number of Residues	16
Details	ALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. IPRSDLpeRLvQNrSF

Chain	Residue	Details
A	ILE272-PHE287

---

site_id	PS00798
Number of Residues	18
Details	ALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRLFDGAedygnEkeVG

Chain	Residue	Details
A	GLY42-GLY59

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton donor"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	80
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12733986","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15320875","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16336198","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Site: {"description":"Lowers pKa of active site Tyr","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	LYS81
A	ASP47
A	HIS114
A	TYR52

---

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

Chain	Residue	Details
B	LYS81
B	ASP47
B	HIS114
B	TYR52

---

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1mrq

Chain	Residue	Details
C	LYS81
C	ASP47
C	HIS114
C	TYR52

---

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1mrq

Chain	Residue	Details
D	LYS81
D	ASP47
D	HIS114
D	TYR52

---

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1mrq

Chain	Residue	Details
A	LYS81
A	TYR52

---

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1mrq

Chain	Residue	Details
B	LYS81
B	TYR52

---

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1mrq

Chain	Residue	Details
C	LYS81
C	TYR52

---

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1mrq

Chain	Residue	Details
D	LYS81
D	TYR52

---