2D8A

Crystal Structure of PH0655 from Pyrococcus horikoshii OT3

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0006566	biological_process	threonine metabolic process
A	0006567	biological_process	threonine catabolic process
A	0008270	molecular_function	zinc ion binding
A	0008743	molecular_function	L-threonine 3-dehydrogenase activity
A	0016491	molecular_function	oxidoreductase activity
A	0016597	molecular_function	amino acid binding
A	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0019518	biological_process	L-threonine catabolic process to glycine
A	0030554	molecular_function	adenyl nucleotide binding
A	0043168	molecular_function	anion binding
A	0046872	molecular_function	metal ion binding
A	0051262	biological_process	protein tetramerization
A	0051289	biological_process	protein homotetramerization
A	0070401	molecular_function	NADP+ binding
A	0070403	molecular_function	NAD+ binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 501

Chain	Residue
A	CYS42
A	HIS67
A	GLU68
A	HOH762

---

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN A 502

Chain	Residue
A	GLU92
A	GLU152
A	HIS295

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 503

Chain	Residue
A	HOH634
A	HOH635
A	HOH763
A	HIS94
A	HIS295

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 504

Chain	Residue
A	GLU127
A	GLU221
A	HOH764
A	HOH765

---

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN A 505

Chain	Residue
A	GLU222
A	ASP326
A	HOH766

---

site_id	AC6
Number of Residues	23
Details	BINDING SITE FOR RESIDUE NAD A 401

Chain	Residue
A	GLY175
A	GLY177
A	PRO178
A	LEU179
A	SER198
A	GLU199
A	PRO200
A	ARG204
A	PHE243
A	SER244
A	ALA246
A	LEU266
A	GLY267
A	LEU268
A	ILE282
A	ILE291
A	THR292
A	HOH509
A	HOH516
A	HOH580
A	HOH592
A	HOH732
A	HOH747

---

Functional Information from PROSITE/UniProt

site_id	PS00059
Number of Residues	15
Details	ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEvAGEvveiGpgV

Chain	Residue	Details
A	GLY66-VAL80

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Charge relay system => ECO:0000305|PubMed:18390572

Chain	Residue	Details
A	THR44
A	HIS47

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00627, ECO:0000269|Ref.5, ECO:0000305|PubMed:17188300, ECO:0000305|PubMed:18390572, ECO:0007744|PDB:2D8A

Chain	Residue	Details
A	CYS42
A	HIS67
A	GLU68

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00627, ECO:0000269|PubMed:17188300, ECO:0007744|PDB:2DFV

Chain	Residue	Details
A	CYS97
A	CYS100
A	CYS103
A	CYS111

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:17188300, ECO:0000269|Ref.5

Chain	Residue	Details
A	LEU179

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:17188300, ECO:0000269|Ref.5, ECO:0007744|PDB:2D8A, ECO:0007744|PDB:2DFV

Chain	Residue	Details
A	GLU199
A	ARG204

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|Ref.5, ECO:0007744|PDB:2D8A

Chain	Residue	Details
A	LEU266
A	ILE291

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	SITE: Important for catalytic activity for the proton relay mechanism but does not participate directly in the coordination of zinc atom => ECO:0000305|PubMed:18390572

Chain	Residue	Details
A	GLU152

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1teh

Chain	Residue	Details
A	THR44
A	GLY43

---

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

Chain	Residue	Details
A	THR44
A	HIS47

---