5MW1

cryoEM structure of crenactin double helical filament at 3.8A resolution

Replaces:  5LY4

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005856	cellular_component	cytoskeleton
A	0016787	molecular_function	hydrolase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005856	cellular_component	cytoskeleton
B	0016787	molecular_function	hydrolase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005856	cellular_component	cytoskeleton
C	0016787	molecular_function	hydrolase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005856	cellular_component	cytoskeleton
D	0016787	molecular_function	hydrolase activity
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0005856	cellular_component	cytoskeleton
E	0016787	molecular_function	hydrolase activity
F	0005524	molecular_function	ATP binding
F	0005737	cellular_component	cytoplasm
F	0005856	cellular_component	cytoskeleton
F	0016787	molecular_function	hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	binding site for residue ADP B 501

Chain	Residue
B	GLY19
B	GLU235
B	LYS238
B	ARG239
B	GLY354
B	ALA355
B	SER357
B	TRP358
B	GLN399
B	THR20
B	SER21
B	TYR22
B	LYS24
B	GLN164
B	GLY183
B	HIS184
B	GLY185

---

site_id	AC2
Number of Residues	17
Details	binding site for residue ADP A 501

Chain	Residue
A	GLY19
A	THR20
A	SER21
A	TYR22
A	LYS24
A	GLN164
A	GLY183
A	HIS184
A	GLY185
A	GLU235
A	LYS238
A	ARG239
A	GLY354
A	ALA355
A	SER357
A	TRP358
A	GLN399

---

site_id	AC3
Number of Residues	17
Details	binding site for residue ADP C 501

Chain	Residue
C	GLY19
C	THR20
C	SER21
C	TYR22
C	LYS24
C	GLN164
C	GLY183
C	HIS184
C	GLY185
C	GLU235
C	LYS238
C	ARG239
C	GLY354
C	ALA355
C	SER357
C	TRP358
C	GLN399

---

site_id	AC4
Number of Residues	17
Details	binding site for residue ADP D 501

Chain	Residue
D	GLY19
D	THR20
D	SER21
D	TYR22
D	LYS24
D	GLN164
D	GLY183
D	HIS184
D	GLY185
D	GLU235
D	LYS238
D	ARG239
D	GLY354
D	ALA355
D	SER357
D	TRP358
D	GLN399

---

site_id	AC5
Number of Residues	17
Details	binding site for residue ADP E 501

Chain	Residue
E	GLY19
E	THR20
E	SER21
E	TYR22
E	LYS24
E	GLN164
E	GLY183
E	HIS184
E	GLY185
E	GLU235
E	LYS238
E	ARG239
E	GLY354
E	ALA355
E	SER357
E	TRP358
E	GLN399

---

site_id	AC6
Number of Residues	17
Details	binding site for residue ADP F 501

Chain	Residue
F	SER357
F	TRP358
F	GLN399
F	GLY19
F	THR20
F	SER21
F	TYR22
F	LYS24
F	GLN164
F	GLY183
F	HIS184
F	GLY185
F	GLU235
F	LYS238
F	ARG239
F	GLY354
F	ALA355

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	BINDING: BINDING => ECO:0000305|PubMed:24486010, ECO:0000305|PubMed:24531483, ECO:0000305|PubMed:27852434

Chain	Residue	Details
B	THR20
C	GLY182
C	GLU235
C	GLY354
D	THR20
D	GLY182
D	GLU235
D	GLY354
E	THR20
E	GLY182
E	GLU235
B	GLY182
E	GLY354
F	THR20
F	GLY182
F	GLU235
F	GLY354
B	GLU235
B	GLY354
A	THR20
A	GLY182
A	GLU235
A	GLY354
C	THR20

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000305|PubMed:27852434

Chain	Residue	Details
B	GLN399
A	GLN399
C	GLN399
D	GLN399
E	GLN399
F	GLN399

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