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6QPW

Structural basis of cohesin ring opening

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0007062biological_processsister chromatid cohesion
A0008278cellular_componentcohesin complex
A0016887molecular_functionATP hydrolysis activity
C0005524molecular_functionATP binding
C0016887molecular_functionATP hydrolysis activity
E0005524molecular_functionATP binding
E0007062biological_processsister chromatid cohesion
E0008278cellular_componentcohesin complex
E0016887molecular_functionATP hydrolysis activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue MG A 301
ChainResidue
ASER40
AGLN177
AAGS302

site_idAC2
Number of Residues21
Detailsbinding site for residue AGS A 302
ChainResidue
AGLY38
ALYS39
ASER40
AASN41
AASP64
AILE66
AARG68
AGLN177
AMG301
CGLN1125
CLEU1126
CSER1127
CGLY1129
EGLU1198
EARG1246
ALYS13
ASER14
APRO34
AASN35
AGLY36
ASER37

site_idAC3
Number of Residues3
Detailsbinding site for residue MG E 1301
ChainResidue
CSER39
CGLN148
EAGS1302

site_idAC4
Number of Residues19
Detailsbinding site for residue AGS E 1302
ChainResidue
CLYS12
CASN34
CGLY35
CSER36
CGLY37
CLYS38
CSER39
CASN40
CGLY63
CILE65
CGLN67
CGLN148
CLYS1205
ELYS1161
EHIS1168
ESER1170
EGLY1171
EGLY1172
EMG1301

Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGEKTMAALALLF
ChainResidueDetails
ELEU1169-PHE1183

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
CGLY32

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18614053
ChainResidueDetails
CLYS112
CLYS113

226707

PDB entries from 2024-10-30

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