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4N59

The Crystal Structure of Pectocin M2 at 2.3 Angstroms

Functional Information from GO Data
ChainGOidnamespacecontents
A0009055molecular_functionelectron transfer activity
A0022900biological_processelectron transport chain
A0042742biological_processdefense response to bacterium
A0046872molecular_functionmetal ion binding
A0051536molecular_functioniron-sulfur cluster binding
A0051537molecular_function2 iron, 2 sulfur cluster binding
B0009055molecular_functionelectron transfer activity
B0022900biological_processelectron transport chain
B0042742biological_processdefense response to bacterium
B0046872molecular_functionmetal ion binding
B0051536molecular_functioniron-sulfur cluster binding
B0051537molecular_function2 iron, 2 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES A 301
ChainResidue
ASER37
ACYS38
AARG39
AGLY41
AALA42
ACYS43
ACYS46
ACYS75

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
AHIS235
AARG236
AHOH412
AHOH423
ATHR234

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 A 303
ChainResidue
AARG258

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES B 301
ChainResidue
BSER37
BCYS38
BARG39
BGLY41
BALA42
BCYS43
BCYS46
BCYS75

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 302
ChainResidue
BASN147
BGLY261
BGLU262

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 303
ChainResidue
BARG258
BPRO260

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 304
ChainResidue
BGLY197
BASN198
BHOH419

Functional Information from PROSITE/UniProt
site_idPS00197
Number of Residues9
Details2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CRAGACSSC
ChainResidueDetails
ACYS38-CYS46

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PDB entries from 2024-07-10

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