5H7X

Crystal structure of the complex of Phosphopantetheine adenylyltransferase from Acinetobacter baumannii with 2-hydroxy-1,2,3-propane tricarboxylate at 1.76 A resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004595	molecular_function	pantetheine-phosphate adenylyltransferase activity
A	0005737	cellular_component	cytoplasm
A	0009058	biological_process	biosynthetic process
A	0015937	biological_process	coenzyme A biosynthetic process
B	0003824	molecular_function	catalytic activity
B	0004595	molecular_function	pantetheine-phosphate adenylyltransferase activity
B	0005737	cellular_component	cytoplasm
B	0009058	biological_process	biosynthetic process
B	0015937	biological_process	coenzyme A biosynthetic process
C	0003824	molecular_function	catalytic activity
C	0004595	molecular_function	pantetheine-phosphate adenylyltransferase activity
C	0005737	cellular_component	cytoplasm
C	0009058	biological_process	biosynthetic process
C	0015937	biological_process	coenzyme A biosynthetic process
D	0003824	molecular_function	catalytic activity
D	0004595	molecular_function	pantetheine-phosphate adenylyltransferase activity
D	0005737	cellular_component	cytoplasm
D	0009058	biological_process	biosynthetic process
D	0015937	biological_process	coenzyme A biosynthetic process
E	0003824	molecular_function	catalytic activity
E	0004595	molecular_function	pantetheine-phosphate adenylyltransferase activity
E	0005737	cellular_component	cytoplasm
E	0009058	biological_process	biosynthetic process
E	0015937	biological_process	coenzyme A biosynthetic process
F	0003824	molecular_function	catalytic activity
F	0004595	molecular_function	pantetheine-phosphate adenylyltransferase activity
F	0005737	cellular_component	cytoplasm
F	0009058	biological_process	biosynthetic process
F	0015937	biological_process	coenzyme A biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	binding site for residue CIT A 201

Chain	Residue
A	GLY10
A	HOH334
A	HOH382
A	THR11
A	PHE12
A	HIS19
A	SER129
A	SER130
A	THR131
A	HOH305
A	HOH316

---

site_id	AC2
Number of Residues	10
Details	binding site for residue CIT B 201

Chain	Residue
B	GLY10
B	THR11
B	PHE12
B	HIS19
B	SER129
B	SER130
B	THR131
B	HOH302
B	HOH303
B	HOH312

---

site_id	AC3
Number of Residues	13
Details	binding site for residue CIT C 201

Chain	Residue
C	GLY10
C	THR11
C	PHE12
C	HIS19
C	SER129
C	SER130
C	THR131
C	HOH301
C	HOH304
C	HOH306
C	HOH307
C	HOH337
C	HOH370

---

site_id	AC4
Number of Residues	11
Details	binding site for residue CIT D 201

Chain	Residue
D	GLY10
D	THR11
D	PHE12
D	HIS19
D	SER129
D	SER130
D	THR131
D	HOH303
D	HOH306
D	HOH325
D	HOH336

---

site_id	AC5
Number of Residues	12
Details	binding site for residue CIT E 201

Chain	Residue
E	GLY10
E	THR11
E	PHE12
E	HIS19
E	ARG92
E	SER129
E	SER130
E	THR131
E	HOH301
E	HOH325
E	HOH338
E	HOH384

---

site_id	AC6
Number of Residues	12
Details	binding site for residue CIT F 201

Chain	Residue
F	GLY10
F	THR11
F	PHE12
F	HIS19
F	SER129
F	SER130
F	THR131
F	HOH301
F	HOH303
F	HOH308
F	HOH310
F	HOH343

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI2
Number of Residues	90
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	6
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---