Structure of PDB 2ot0 Chain B Binding Site BS01

Receptor Information

>2ot0 Chain B (length=357) Species: 9986 (Oryctolagus cuniculus)

PHSHPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTEN
TEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSK
GGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCV
LKIGEHTPSALAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKR
CQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKYSHEEIAM
ATVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFS
YGRALQASALKAWGGKKENLKAAQEEYVKRALANSLACQGKYTPSGQASL
FISNHAY

Ligand information

>2ot0 Chain F (length=4) Species: 9606 (Homo sapiens)

DEWD

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2ot0 A hydrophobic pocket in the active site of glycolytic aldolase mediates interactions with wiskott-Aldrich syndrome protein.
• Resolution: 2.05 Å
• Binding residue (original residue number in PDB): E34 S38 K41 R42 K146 R148 R303 Q306
• Binding residue (residue number reindexed from 1): E34 S38 K41 R42 K146 R148 R303 Q306

Enzymatic activity

• Catalytic site (original residue number in PDB): D33 K146 E187 E189 K229 S300 Y363
• Catalytic site (residue number reindexed from 1): D33 K146 E187 E189 K229 S300 Y357
• Enzyme Commision number: 4.1.2.13: fructose-bisphosphate aldolase.

Gene Ontology

Molecular Function

• GO:0004332 fructose-bisphosphate aldolase activity
• GO:0005515 protein binding
• GO:0016829 lyase activity

Biological Process

• GO:0006096 glycolytic process
• GO:0030335 positive regulation of cell migration
• GO:0030388 fructose 1,6-bisphosphate metabolic process
• GO:0034316 negative regulation of Arp2/3 complex-mediated actin nucleation
• GO:0051289 protein homotetramerization

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol
• GO:0031430 M band
• GO:0031674 I band

External links

• PDB: RCSB:2ot0, PDBe:2ot0, PDBj:2ot0
• PDBsum: 2ot0
• PubMed: 17329259
• UniProt: P00883|ALDOA_RABIT Fructose-bisphosphate aldolase A (Gene Name=ALDOA)