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1G9A

CRYSTAL STRUCTURE OF CLOSTRIDIUM BOTULINUM NEUROTOXIN B COMPLEXED WITH AN INHIBITOR (EXPERIMENT 3)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0008289molecular_functionlipid binding
A0008320molecular_functionprotein transmembrane transporter activity
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0020002cellular_componenthost cell plasma membrane
A0030430cellular_componenthost cell cytoplasm
A0033644cellular_componenthost cell membrane
A0035821biological_processmodulation of process of another organism
A0044161cellular_componenthost cell cytoplasmic vesicle
A0044164cellular_componenthost cell cytosol
A0044221cellular_componenthost cell synapse
A0044231cellular_componenthost cell presynaptic membrane
A0046872molecular_functionmetal ion binding
A0071806biological_processprotein transmembrane transport
A0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1291
ChainResidue
AHIS229
AHIS233
AHOH1619
AHOH1706

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN A 1294
ChainResidue
AGLN258
ABAB1292

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE BAB A 1292
ChainResidue
ATYR372
APHE373
ASER374
AASP375
ASER376
AGLU451
ALEU453
APHE454
APHE455
ATHR709
AGLN710
ATHR713
AZN1294
AHOH1492
AHOH1722
AASP68
AGLN258
AARG369

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE BAB A 1293
ChainResidue
AASN203
AARG217
AASP375
ALEU377
AASP452
APHE537
ALEU540
AGLU716
ALYS720
ATYR724
AHOH1644

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. ILMHELIHVL
ChainResidueDetails
AILE226-LEU235

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095
ChainResidueDetails
ALEU231

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:10932256, ECO:0000305|PubMed:1429690, ECO:0007744|PDB:1EPW, ECO:0007744|PDB:1F31, ECO:0007744|PDB:2NP0
ChainResidueDetails
AGLU230
AVAL234

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10932256, ECO:0007744|PDB:1EPW, ECO:0007744|PDB:1F31, ECO:0007744|PDB:2NP0
ChainResidueDetails
ALEU268

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:4KBB
ChainResidueDetails
ATHR1025

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10932256, ECO:0000305|PubMed:14731268, ECO:0007744|PDB:4KBB
ChainResidueDetails
AGLU1189
AHIS1240

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 626
ChainResidueDetails
AGLU230metal ligand
ALEU231proton acceptor, proton donor
AVAL234metal ligand
ALEU268metal ligand
AALA370electrostatic stabiliser

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PDB entries from 2024-04-24

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