2DBQ

Crystal Structure of Glyoxylate Reductase (PH0597) from Pyrococcus horikoshii OT3, Complexed with NADP (I41)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
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	0016618	molecular_function	hydroxypyruvate reductase [NAD(P)H] activity
A	0030267	molecular_function	glyoxylate reductase (NADPH) activity
A	0047964	molecular_function	glyoxylate reductase (NADH) activity
A	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 601

Chain	Residue
A	LYS41
A	TYR78
A	ASN95
A	ARG160
A	HOH612
A	HOH641
A	HOH673

---

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 A 602

Chain	Residue
A	VAL76
A	GLY77
A	LEU100
A	ARG241
A	HIS288
A	NAP401
A	GOL501
A	HOH646
A	LEU53
A	ALA75

---

site_id	AC3
Number of Residues	37
Details	BINDING SITE FOR RESIDUE NAP A 401

Chain	Residue
A	LYS42
A	VAL76
A	THR104
A	GLY157
A	LEU158
A	GLY159
A	ARG160
A	ILE161
A	SER180
A	ARG181
A	THR182
A	ALA211
A	VAL212
A	PRO213
A	THR218
A	ILE239
A	ALA240
A	ARG241
A	ASP265
A	VAL266
A	HIS288
A	GLY290
A	SER291
A	SO4602
A	HOH603
A	HOH604
A	HOH605
A	HOH611
A	HOH612
A	HOH644
A	HOH646
A	HOH648
A	HOH651
A	HOH667
A	HOH682
A	HOH795
A	HOH814

---

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 501

Chain	Residue
A	MSE52
A	LEU53
A	TYR74
A	ALA75
A	TRP138
A	HIS288
A	MSE300
A	SO4602
A	HOH828

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 502

Chain	Residue
A	PRO35
A	ARG36
A	GLU37
A	GLU324
A	HOH830

---

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 503

Chain	Residue
A	LYS243
A	PHE267
A	GLU268
A	GLU269
A	GLU270
A	HOH630
A	HOH658
A	HOH694
A	HOH723

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 504

Chain	Residue
A	LYS151
A	ASP206
A	HOH619
A	HOH631
A	HOH759

---

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 505

Chain	Residue
A	PHE125
A	ARG134
A	PHE143
A	HOH657
A	HOH829
A	HOH964

---

Functional Information from PROSITE/UniProt

site_id	PS00065
Number of Residues	28
Details	D_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. IGIIGlGRIGqaiakrakgfnmr.ILyYS

Chain	Residue	Details
A	ILE153-SER180

---

site_id	PS00671
Number of Residues	17
Details	D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. MKkTaILINiARGkVVD

Chain	Residue	Details
A	MSE230-ASP246

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of glyoxylate reductase (ph0597) from Pyrococcus horikoshii OT3, complexed with nadp (i41).","authoringGroup":["RIKEN structural genomics initiative (RSGI)"]}}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 1gdh

Chain	Residue	Details
A	LYS243
A	ASP265
A	ARG241
A	GLU270
A	HIS288

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1gdh

Chain	Residue	Details
A	GLU270
A	HIS288

---