2E5W

Crystal structure of spermidine synthase from Pyrococcus horikoshii OT3

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004766	molecular_function	spermidine synthase activity
A	0005737	cellular_component	cytoplasm
A	0006596	biological_process	polyamine biosynthetic process
A	0008295	biological_process	spermidine biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
B	0003824	molecular_function	catalytic activity
B	0004766	molecular_function	spermidine synthase activity
B	0005737	cellular_component	cytoplasm
B	0006596	biological_process	polyamine biosynthetic process
B	0008295	biological_process	spermidine biosynthetic process
B	0016740	molecular_function	transferase activity
B	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
C	0003824	molecular_function	catalytic activity
C	0004766	molecular_function	spermidine synthase activity
C	0005737	cellular_component	cytoplasm
C	0006596	biological_process	polyamine biosynthetic process
C	0008295	biological_process	spermidine biosynthetic process
C	0016740	molecular_function	transferase activity
C	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups
D	0003824	molecular_function	catalytic activity
D	0004766	molecular_function	spermidine synthase activity
D	0005737	cellular_component	cytoplasm
D	0006596	biological_process	polyamine biosynthetic process
D	0008295	biological_process	spermidine biosynthetic process
D	0016740	molecular_function	transferase activity
D	0016765	molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACT B 1101

Chain	Residue
A	HOH1130
B	SER231
B	HOH1115
B	HOH1123

---

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ACT A 1102

Chain	Residue
A	SER231
A	HOH1103

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACT D 1103

Chain	Residue
D	HOH1107
C	HOH1119
C	HOH1130
D	SER231

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACT C 1104

Chain	Residue
C	SER231
C	HOH1107
C	HOH1192

---

site_id	AC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE AG3 A 1001

Chain	Residue
A	GLU8
A	TYR10
A	VAL52
A	GLN53
A	TYR62
A	HIS63
A	ASP87
A	ASP161
A	SER162
A	ASP164
A	GLN194
A	TYR229
A	TRP233
A	MTA1003

---

site_id	AC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE AG3 C 1002

Chain	Residue
C	GLU8
C	TYR10
C	VAL52
C	GLN53
C	TYR62
C	HIS63
C	ASP87
C	ASP161
C	SER162
C	ASP164
C	GLN194
C	TYR229
C	TRP233
C	MTA1004

---

site_id	AC7
Number of Residues	22
Details	BINDING SITE FOR RESIDUE MTA A 1003

Chain	Residue
A	GLN32
A	ILE48
A	GLN53
A	GLY84
A	GLY85
A	GLY86
A	ASP87
A	VAL106
A	GLU107
A	ILE108
A	ASP109
A	VAL112
A	GLY143
A	ASP144
A	GLY145
A	ASP161
A	SER162
A	THR163
A	PRO168
A	ALA169
A	LEU172
A	AG31001

---

site_id	AC8
Number of Residues	20
Details	BINDING SITE FOR RESIDUE MTA C 1004

Chain	Residue
C	GLN32
C	ILE48
C	GLN53
C	GLY84
C	GLY85
C	GLY86
C	ASP87
C	VAL106
C	GLU107
C	ILE108
C	ASP109
C	VAL112
C	ASP144
C	GLY145
C	ASP161
C	SER162
C	THR163
C	PRO168
C	ALA169
C	AG31002

---

Functional Information from PROSITE/UniProt

site_id	PS01330
Number of Residues	14
Details	PABS_1 Polyamine biosynthesis (PABS) domain signature. VLIIGGGdGgaIrE

Chain	Residue	Details
A	VAL80-GLU93

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	466
Details	Domain: {"description":"PABS","evidences":[{"source":"HAMAP-Rule","id":"MF_00198","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00198","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of spermidine synthase from Pyrococcus horikoshII OT3.","authoringGroup":["RIKEN structural genomics initiative (RSGI)"]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00198","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of spermidine synthase from Pyrococcus horikoshII OT3.","authoringGroup":["RIKEN structural genomics initiative (RSGI)"]}},{"source":"PDB","id":"2E5W","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00198","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of spermidine synthase from Pyrococcus horikoshII OT3.","authoringGroup":["RIKEN structural genomics initiative (RSGI)"]}},{"source":"PDB","id":"2E5W","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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