2I9P

Crystal structure of human hydroxyisobutyrate dehydrogenase complexed with NAD+

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008442	molecular_function	3-hydroxyisobutyrate dehydrogenase activity
A	0016491	molecular_function	oxidoreductase activity
A	0050661	molecular_function	NADP binding
A	0051287	molecular_function	NAD binding
B	0008442	molecular_function	3-hydroxyisobutyrate dehydrogenase activity
B	0016491	molecular_function	oxidoreductase activity
B	0050661	molecular_function	NADP binding
B	0051287	molecular_function	NAD binding
C	0008442	molecular_function	3-hydroxyisobutyrate dehydrogenase activity
C	0016491	molecular_function	oxidoreductase activity
C	0050661	molecular_function	NADP binding
C	0051287	molecular_function	NAD binding
D	0008442	molecular_function	3-hydroxyisobutyrate dehydrogenase activity
D	0016491	molecular_function	oxidoreductase activity
D	0050661	molecular_function	NADP binding
D	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE NAD A 500

Chain	Residue
A	ILE45
A	MET102
A	LEU103
A	PRO104
A	ASN108
A	THR134
A	VAL159
A	GLY161
A	GLY162
A	LYS209
A	PHE277
A	GLY46
A	LEU281
A	LYS284
A	ASP285
A	GLY48
A	ASN49
A	MET50
A	TYR68
A	ASP69
A	VAL70
A	PHE71

---

site_id	AC2
Number of Residues	21
Details	BINDING SITE FOR RESIDUE NAD B 500

Chain	Residue
B	ILE45
B	GLY46
B	GLY48
B	ASN49
B	MET50
B	TYR68
B	ASP69
B	VAL70
B	MET102
B	LEU103
B	PRO104
B	ASN108
B	THR134
B	VAL159
B	GLY161
B	GLY162
B	LYS209
B	PHE277
B	LEU281
B	LYS284
B	ASP285

---

site_id	AC3
Number of Residues	21
Details	BINDING SITE FOR RESIDUE NAD C 500

Chain	Residue
C	ILE45
C	GLY46
C	GLY48
C	ASN49
C	MET50
C	GLY51
C	TYR68
C	ASP69
C	VAL70
C	PHE71
C	MET102
C	LEU103
C	PRO104
C	ASN108
C	THR134
C	VAL159
C	GLY161
C	GLY162
C	LYS209
C	LYS284
C	ASP285

---

site_id	AC4
Number of Residues	20
Details	BINDING SITE FOR RESIDUE NAD D 500

Chain	Residue
D	GLY46
D	GLY48
D	ASN49
D	MET50
D	TYR68
D	ASP69
D	VAL70
D	PHE71
D	MET102
D	LEU103
D	PRO104
D	ASN108
D	THR134
D	VAL159
D	GLY161
D	GLY162
D	LYS209
D	PHE277
D	LYS284
D	ASP285

---

Functional Information from PROSITE/UniProt

site_id	PS00895
Number of Residues	14
Details	3_HYDROXYISOBUT_DH 3-hydroxyisobutyrate dehydrogenase signature. FIGLGnMGnpMAkN

Chain	Residue	Details
A	PHE44-ASN57

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: ACT_SITE => ECO:0000250

Chain	Residue	Details
A	LYS209
B	LYS209
C	LYS209
D	LYS209

---

site_id	SWS_FT_FI2
Number of Residues	20
Details	BINDING: BINDING => ECO:0000269|Ref.12

Chain	Residue	Details
A	MET40
B	LYS284
C	MET40
C	LEU103
C	ASN108
C	THR134
C	LYS284
D	MET40
D	LEU103
D	ASN108
D	THR134
A	LEU103
D	LYS284
A	ASN108
A	THR134
A	LYS284
B	MET40
B	LEU103
B	ASN108
B	THR134

---

site_id	SWS_FT_FI3
Number of Residues	24
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99L13

Chain	Residue	Details
A	LYS60
B	LYS238
B	LYS242
B	LYS321
C	LYS60
C	LYS76
C	LYS149
C	LYS238
C	LYS242
C	LYS321
D	LYS60
A	LYS76
D	LYS76
D	LYS149
D	LYS238
D	LYS242
D	LYS321
A	LYS149
A	LYS238
A	LYS242
A	LYS321
B	LYS60
B	LYS76
B	LYS149

---

site_id	SWS_FT_FI4
Number of Residues	12
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q99L13

Chain	Residue	Details
A	LYS95
D	LYS95
D	LYS141
D	LYS297
A	LYS141
A	LYS297
B	LYS95
B	LYS141
B	LYS297
C	LYS95
C	LYS141
C	LYS297

---

site_id	SWS_FT_FI5
Number of Residues	8
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q99L13

Chain	Residue	Details
A	LYS121
A	LYS145
B	LYS121
B	LYS145
C	LYS121
C	LYS145
D	LYS121
D	LYS145

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