Structure of PDB 3kyd Chain B

Receptor sequence
>3kydB (length=477) Species: 9606 (Homo sapiens) [Search protein sequence]
SRGLPRELAEAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTID
VSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYHDSIMNPDYNV
EFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKK
GVTECYECHPKPTQRTFPGCTIRNTPSEPIHCIVWAKYLFNQLFTKEWAK
STGYDPVKLFTKLFKDDIRYLLTMDKLWRKRKPPVPLDWAEVQSQDQQVL
DVKSYARLFSKSIETLRVHLAEKDKDDPSAMDFVTSAANLRMHIFSMNMK
SRFDIKSMAGNIIPAIATTNAVIAGLIVLEGLKILSGKIDQCRTIFLNKQ
PNPRKKLLVPCALDPPNPNCYVCASKPEVTVRLNVHKVTVLTLQDKIVKE
KFAMVAPDVQIEDGKGTILISSEEGETEANNHKKLSEFGIRNGSRLQADD
FLQDYTLLINILHSEDLGKDVEFEVVG
3D structure
PDB3kyd Active site remodelling accompanies thioester bond formation in the SUMO E1.
ChainB
Resolution2.61 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D117 C173 T174 R176
Catalytic site (residue number reindexed from 1) D114 C170 T171 R173
Enzyme Commision number 2.3.2.-
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ZN B C158 C161 C441 C444 C155 C158 C370 C373
BS02 VMX B I28 D48 L49 K72 S95 I96 L116 D117 N118 C173 R176 I25 D45 L46 K69 S92 I93 L113 D114 N115 C170 R173
Gene Ontology
Molecular Function
GO:0008641 ubiquitin-like modifier activating enzyme activity
GO:0019948 SUMO activating enzyme activity
Biological Process
GO:0016925 protein sumoylation

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Molecular Function
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Biological Process
External links
PDB RCSB:3kyd, PDBe:3kyd, PDBj:3kyd
PDBsum3kyd
PubMed20164921
UniProtQ9UBT2|SAE2_HUMAN SUMO-activating enzyme subunit 2 (Gene Name=UBA2)

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