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2XSZ

The dodecameric human RuvBL1:RuvBL2 complex with truncated domains II

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0008094molecular_functionATP-dependent activity, acting on DNA
A0016887molecular_functionATP hydrolysis activity
B0005524molecular_functionATP binding
B0008094molecular_functionATP-dependent activity, acting on DNA
B0016887molecular_functionATP hydrolysis activity
C0005524molecular_functionATP binding
C0008094molecular_functionATP-dependent activity, acting on DNA
C0016887molecular_functionATP hydrolysis activity
D0005524molecular_functionATP binding
D0008094molecular_functionATP-dependent activity, acting on DNA
D0016887molecular_functionATP hydrolysis activity
E0005524molecular_functionATP binding
E0008094molecular_functionATP-dependent activity, acting on DNA
E0016887molecular_functionATP hydrolysis activity
F0005524molecular_functionATP binding
F0008094molecular_functionATP-dependent activity, acting on DNA
F0016887molecular_functionATP hydrolysis activity
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ATP A 501
ChainResidue
ASER31
ALYS90
ATHR91
AALA92
ATYR277
AILE285
ALEU314
AARG315
FASP267
AHIS32
AHIS34
AGLY52
ALEU53
AVAL54
AGLY87
ATHR88
AGLY89

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ATP B 501
ChainResidue
BSER31
BHIS32
BHIS34
BGLY52
BLEU53
BVAL54
BGLY87
BTHR88
BGLY89
BLYS90
BTHR91
BALA92
BTYR277
BILE285
BLEU314
BARG315
DASP267

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ATP C 501
ChainResidue
CSER31
CHIS32
CHIS34
CGLY52
CLEU53
CVAL54
CGLY87
CTHR88
CGLY89
CLYS90
CTHR91
CALA92
CTYR277
CILE285
CLEU314
CARG315
EASP267

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ATP D 501
ChainResidue
AASP267
DALA39
DHIS40
DHIS42
DILE43
DGLY60
DMSE61
DVAL62
DGLY95
DTHR96
DGLY97
DLYS98
DTHR99
DALA100
DASP214
DTYR277
DILE285
DLEU314

site_idAC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ATP E 501
ChainResidue
EALA39
EHIS40
EHIS42
EILE43
EGLY60
EMSE61
EVAL62
EGLY95
ETHR96
EGLY97
ELYS98
ETHR99
EALA100
EASP214
ETYR277
EILE285
ELEU314

site_idAC6
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ATP F 501
ChainResidue
FTHR99
FALA100
FASP214
FTYR277
FILE285
FLEU314
CASP267
FALA39
FHIS40
FHIS42
FILE43
FGLY60
FMSE61
FVAL62
FGLN64
FGLY95
FTHR96
FGLY97
FLYS98

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING:
ChainResidueDetails
DGLY92
EGLY92
FGLY92

site_idSWS_FT_FI2
Number of Residues3
DetailsMOD_RES: N-acetylalanine => ECO:0000269|Ref.14, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
ChainResidueDetails
DALA17
EALA17
FALA17

site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
DSER352
ESER352
FSER352

site_idSWS_FT_FI4
Number of Residues12
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
DLYS24
FLYS359
FLYS371
ALYS356
DLYS359
DLYS371
ELYS24
CLYS356
ELYS359
ELYS371
FLYS24

site_idSWS_FT_FI5
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
AILE239
BILE239
CILE239

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PDB entries from 2024-07-24

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