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1Z7L

Crystal structure of fragment of mouse ubiquitin-activating enzyme

Functional Information from GO Data
ChainGOidnamespacecontents
A0008641molecular_functionubiquitin-like modifier activating enzyme activity
B0008641molecular_functionubiquitin-like modifier activating enzyme activity
C0008641molecular_functionubiquitin-like modifier activating enzyme activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE TBR A 999
ChainResidue
AGLN646
AARG649
AASP650

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE TBR B 1000
ChainResidue
BGLN646
BARG649
BASP650

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE TBR C 1001
ChainResidue
CGLU653
CGLN646
CARG649
CASP650

Functional Information from PROSITE/UniProt
site_idPS00865
Number of Residues9
DetailsUBIQUITIN_ACTIVAT_2 Ubiquitin-activating enzyme active site. PICTLKnFP
ChainResidueDetails
APRO630-PRO638

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Glycyl thioester intermediate => ECO:0000255|PROSITE-ProRule:PRU10132
ChainResidueDetails
ACYS632
BCYS632
CCYS632

site_idSWS_FT_FI2
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:23806337
ChainResidueDetails
ALYS671
BLYS671
CLYS671

site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P22314
ChainResidueDetails
ATHR800
BTHR800
CTHR800

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079
ChainResidueDetails
ASER810
ASER835
BSER810
BSER835
CSER810
CSER835

site_idSWS_FT_FI5
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079
ChainResidueDetails
ASER816
ASER820
BSER816
BSER820
CSER816
CSER820

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PDB entries from 2024-11-06

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