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1Z2U

The 1.1A crystallographic structure of ubiquitin-conjugating enzyme (ubc-2) from Caenorhabditis elegans: functional and evolutionary significance

Functional Information from GO Data
ChainGOidnamespacecontents
A0000209biological_processprotein polyubiquitination
A0004842molecular_functionubiquitin-protein transferase activity
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005694cellular_componentchromosome
A0005737cellular_componentcytoplasm
A0006511biological_processubiquitin-dependent protein catabolic process
A0010623biological_processprogrammed cell death involved in cell development
A0016567biological_processprotein ubiquitination
A0016740molecular_functiontransferase activity
A0031625molecular_functionubiquitin protein ligase binding
A0061631molecular_functionubiquitin conjugating enzyme activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 601
ChainResidue
ATHR58
AASP59
ALYS63
AUNX502

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 602
ChainResidue
ASER-1
AARG131
ALYS144
AHOH318

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 603
ChainResidue
ALEU3
AARG131
AHOH315
AHOH356
AHIS0

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 604
ChainResidue
AARG15

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 605
ChainResidue
AGLY-2
AHIS0
ALYS4
AMET147

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 606
ChainResidue
ABU3201
AHOH317
AHOH334

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 701
ChainResidue
ASER-1
AASP112
APRO113
ATYR127
ABU3201

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BU3 A 201
ChainResidue
ASER-1
AASP112
APRO113
APRO115
AASP116
AHOH319
AHOH353
ACL606
ANA701

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BU3 A 202
ChainResidue
AARG15
AHOH383
AHOH404

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE UNX A 501
ChainResidue
AASP28
AASP29
ALEU30
APHE31
AARG139

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE UNX A 502
ChainResidue
ACL601

site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE UNX A 503
ChainResidue
AASP130

site_idBC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE UNX A 504
ChainResidue
ASER22
ATHR36

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE UNX A 505
ChainResidue
ALEU86
AASN114
AHOH364

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE UNX A 506
ChainResidue
AVAL26
AASP29
ASER94
AARG139
AUNX508
AUNX509

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE UNX A 507
ChainResidue
AGLN34
AALA35
ATHR36

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE UNX A 508
ChainResidue
AGLY27
AASP28
AALA96
AARG139
AUNX506

site_idBC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE UNX A 509
ChainResidue
AHIS32
ASER94
AUNX506
AUNX510

site_idCC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE UNX A 510
ChainResidue
AGLN136
AUNX509

Functional Information from PROSITE/UniProt
site_idPS00183
Number of Residues16
DetailsUBC_1 Ubiquitin-conjugating (UBC) active site signature. YHPNInsn.GsICLdiL
ChainResidueDetails
ATYR74-LEU89

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Glycyl thioester intermediate => ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133
ChainResidueDetails
ACYS85

227344

PDB entries from 2024-11-13

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