6QPW

Structural basis of cohesin ring opening

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0007062	biological_process	sister chromatid cohesion
A	0008278	cellular_component	cohesin complex
A	0016887	molecular_function	ATP hydrolysis activity
C	0005524	molecular_function	ATP binding
C	0016887	molecular_function	ATP hydrolysis activity
E	0005524	molecular_function	ATP binding
E	0007062	biological_process	sister chromatid cohesion
E	0008278	cellular_component	cohesin complex
E	0016887	molecular_function	ATP hydrolysis activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue MG A 301

Chain	Residue
A	SER40
A	GLN177
A	AGS302

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site_id	AC2
Number of Residues	21
Details	binding site for residue AGS A 302

Chain	Residue
A	GLY38
A	LYS39
A	SER40
A	ASN41
A	ASP64
A	ILE66
A	ARG68
A	GLN177
A	MG301
C	GLN1125
C	LEU1126
C	SER1127
C	GLY1129
E	GLU1198
E	ARG1246
A	LYS13
A	SER14
A	PRO34
A	ASN35
A	GLY36
A	SER37

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site_id	AC3
Number of Residues	3
Details	binding site for residue MG C 1301

Chain	Residue
C	SER39
C	GLN148
E	AGS1301

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site_id	AC4
Number of Residues	19
Details	binding site for residue AGS E 1301

Chain	Residue
C	LYS12
C	ASN34
C	GLY35
C	SER36
C	GLY37
C	LYS38
C	SER39
C	ASN40
C	GLY63
C	ILE65
C	GLN67
C	GLN148
C	LYS1205
E	LYS1161
E	HIS1168
E	SER1170
E	GLY1171
E	GLY1172
C	MG1301

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Functional Information from PROSITE/UniProt

site_id	PS00211
Number of Residues	15
Details	ABC_TRANSPORTER_1 ABC transporters family signature. LSGGEKTMAALALLF

Chain	Residue	Details
E	LEU1169-PHE1183

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	7
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18614053","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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