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2M9Y

Solution Structure of the Catalytic Domain of HHARI

Functional Information from GO Data
ChainGOidnamespacecontents
A0004842molecular_functionubiquitin-protein transferase activity
A0008270molecular_functionzinc ion binding
A0016567biological_processprotein ubiquitination
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
ACYS344
ACYS347
ACYS362
ACYS367

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 402
ChainResidue
ACYS372
ACYS375
AHIS382
ACYS389

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues31
DetailsZN_FING: RING-type 2; atypical => ECO:0000255|PROSITE-ProRule:PRU01221
ChainResidueDetails
ACYS344-CYS375

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU01221, ECO:0000269|PubMed:21532592, ECO:0000269|PubMed:23707686
ChainResidueDetails
ASER357

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01221, ECO:0000269|PubMed:15236971, ECO:0000269|PubMed:23707686, ECO:0000269|PubMed:24058416, ECO:0007744|PDB:1WD2, ECO:0007744|PDB:2M9Y, ECO:0007744|PDB:4KBL, ECO:0007744|PDB:4KC9
ChainResidueDetails
ACYS344
ACYS347
ACYS362
ACYS367

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01221, ECO:0000269|PubMed:23707686, ECO:0000269|PubMed:24058416, ECO:0007744|PDB:2M9Y, ECO:0007744|PDB:4KBL, ECO:0007744|PDB:4KC9
ChainResidueDetails
ACYS372
ACYS375
AHIS382
ACYS389

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PDB entries from 2024-07-17

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