5DHR

Crystal structure of NAD kinase 1 from Listeria monocytogenes in complex with a novel inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003951	molecular_function	NAD+ kinase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006741	biological_process	NADP biosynthetic process
A	0016301	molecular_function	kinase activity
A	0019674	biological_process	NAD metabolic process
A	0046872	molecular_function	metal ion binding
A	0051287	molecular_function	NAD binding
B	0003951	molecular_function	NAD+ kinase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006741	biological_process	NADP biosynthetic process
B	0016301	molecular_function	kinase activity
B	0019674	biological_process	NAD metabolic process
B	0046872	molecular_function	metal ion binding
B	0051287	molecular_function	NAD binding
C	0003951	molecular_function	NAD+ kinase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0006741	biological_process	NADP biosynthetic process
C	0016301	molecular_function	kinase activity
C	0019674	biological_process	NAD metabolic process
C	0046872	molecular_function	metal ion binding
C	0051287	molecular_function	NAD binding
D	0003951	molecular_function	NAD+ kinase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0006741	biological_process	NADP biosynthetic process
D	0016301	molecular_function	kinase activity
D	0019674	biological_process	NAD metabolic process
D	0046872	molecular_function	metal ion binding
D	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	binding site for residue CIT A 301

Chain	Residue
A	VAL98
A	TYR100
A	HIS173
A	PHE251
A	PRO252
A	PHE253
A	ARG256
A	HOH406

---

site_id	AC2
Number of Residues	13
Details	binding site for residue 5AJ A 302

Chain	Residue
A	GLU123
A	ALA162
A	TYR163
A	SER166
A	HIS223
A	HOH413
C	GLY131
C	PRO132
C	ARG148
C	GLY149
C	ASP150
C	ALA185
A	ASN122

---

site_id	AC3
Number of Residues	7
Details	binding site for residue CIT B 301

Chain	Residue
B	VAL98
B	TYR100
B	HIS173
B	PRO252
B	PHE253
B	ARG256
B	HOH411

---

site_id	AC4
Number of Residues	14
Details	binding site for residue 5AJ B 302

Chain	Residue
B	ASN122
B	GLU123
B	LYS127
B	ALA162
B	TYR163
B	SER166
B	ASP222
B	HIS223
D	GLY131
D	PRO132
D	ARG148
D	GLY149
D	ASP150
D	ALA185

---

site_id	AC5
Number of Residues	4
Details	binding site for residue GOL C 301

Chain	Residue
A	ASP150
C	LYS127
C	ASP150
C	LEU167

---

site_id	AC6
Number of Residues	14
Details	binding site for residue 5AJ C 302

Chain	Residue
A	GLY131
A	PRO132
A	ARG148
A	GLY149
A	ASP150
A	ALA185
C	GLY46
C	LEU49
C	ASN122
C	GLU123
C	ALA162
C	TYR163
C	SER166
C	ASP222

---

site_id	AC7
Number of Residues	12
Details	binding site for residue 5AJ D 301

Chain	Residue
B	GLY131
B	ARG148
B	GLY149
B	ASP150
B	ALA185
D	GLY46
D	ASN122
D	GLU123
D	ALA162
D	TYR163
D	SER166
D	HIS223

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780

Chain	Residue	Details
A	ASP45
B	ASP45
C	ASP45
D	ASP45

---

site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780

Chain	Residue	Details
A	ASP45
B	SER158
B	THR161
B	HIS223
C	ASP45
C	GLY46
C	ASN122
C	SER158
C	THR161
C	HIS223
D	ASP45
A	GLY46
D	GLY46
D	ASN122
D	SER158
D	THR161
D	HIS223
A	ASN122
A	SER158
A	THR161
A	HIS223
B	ASP45
B	GLY46
B	ASN122

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00361

Chain	Residue	Details
A	ARG148
B	ARG148
C	ARG148
D	ARG148

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000305|PubMed:17686780

Chain	Residue	Details
A	ASP150
B	ASP150
C	ASP150
D	ASP150

---