4NTI

Crystal structure of D60N mutant of Arabidopsis ACD11 (accelerated-cell-death 11) complexed with C12 ceramide-1-phosphate (d18:1/12:0) at 2.9 Angstrom resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006869	biological_process	lipid transport
A	0008289	molecular_function	lipid binding
A	0009751	biological_process	response to salicylic acid
A	0015914	biological_process	phospholipid transport
A	0035627	biological_process	ceramide transport
A	0042742	biological_process	defense response to bacterium
A	0120009	biological_process	intermembrane lipid transfer
A	0120013	molecular_function	lipid transfer activity
A	0120014	molecular_function	phospholipid transfer activity
A	0120016	molecular_function	sphingolipid transfer activity
A	0140338	molecular_function	sphingomyelin transfer activity
A	1902387	molecular_function	ceramide 1-phosphate binding
A	1902388	molecular_function	ceramide 1-phosphate transfer activity
A	1902389	biological_process	ceramide 1-phosphate transport
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006869	biological_process	lipid transport
B	0008289	molecular_function	lipid binding
B	0009751	biological_process	response to salicylic acid
B	0015914	biological_process	phospholipid transport
B	0035627	biological_process	ceramide transport
B	0042742	biological_process	defense response to bacterium
B	0120009	biological_process	intermembrane lipid transfer
B	0120013	molecular_function	lipid transfer activity
B	0120014	molecular_function	phospholipid transfer activity
B	0120016	molecular_function	sphingolipid transfer activity
B	0140338	molecular_function	sphingomyelin transfer activity
B	1902387	molecular_function	ceramide 1-phosphate binding
B	1902388	molecular_function	ceramide 1-phosphate transfer activity
B	1902389	biological_process	ceramide 1-phosphate transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE 1PZ A 301

Chain	Residue
A	LEU46
A	ARG103
A	MET110
A	VAL111
A	LEU114
A	ALA131
A	TYR135
A	PHE139
A	HIS143
A	HOH409
A	PHE47
A	LEU50
A	PHE54
A	PHE56
A	ASN60
A	TYR61
A	LYS64
A	ARG99

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE 1PZ A 302

Chain	Residue
A	TRP145
A	1PZ303
B	ALA146
B	ILE147
B	1PZ301

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE 1PZ A 303

Chain	Residue
A	LYS149
A	1PZ302
B	MET59
B	PEG304

---

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 1PZ B 301

Chain	Residue
A	1PZ302
B	ALA53
B	ALA57
B	ASN60
B	LYS64
B	ARG99
B	ARG103
B	PHE139
B	HIS143
B	ALA150
B	LEU153
B	HOH403

---

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG B 304

Chain	Residue
A	TYR156
A	1PZ303

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG B 305

Chain	Residue
A	GLY48
B	PRO159
B	THR160
B	HIS163

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269|PubMed:24412362

Chain	Residue	Details
A	ASN60
B	HIS143
A	LYS64
A	ARG99
A	ARG103
A	HIS143
B	ASN60
B	LYS64
B	ARG99
B	ARG103

---