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1DS1

CRYSTAL STRUCTURE OF CLAVAMINATE SYNTHASE IN COMPLEX WITH FE(II) AND 2-OXOGLUTARATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0016491molecular_functionoxidoreductase activity
A0017000biological_processantibiotic biosynthetic process
A0033050biological_processclavulanic acid biosynthetic process
A0033758molecular_functionclavaminate synthase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 335
ChainResidue
APRO21
AARG22
AHOH459
AHOH517
AHOH711
AHOH723

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 336
ChainResidue
AHOH507
AHOH696
ATHR2
ASER58
AGLU59

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 339
ChainResidue
AARG151
AARG323
AGLY324

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 340
ChainResidue
AARG115
ASER133
ASER134
AARG297
AHOH601

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 A 341
ChainResidue
AHIS144
AGLU146
AHIS279
AAKG330
AHOH487

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE AKG A 330
ChainResidue
ALEU141
AHIS144
AGLU146
ALEU159
ATHR172
AHIS279
AARG281
AARG293
AARG297
AFE2341
AHOH430
AHOH487

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PGO A 331
ChainResidue
AALA17
AALA18
AARG22
ALEU91
ATHR93
AHOH476

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PGO A 332
ChainResidue
AASN54
ASER82
APRO84
APRO86
AARG304
AHOH460

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING:
ChainResidueDetails
AHIS144
AGLU146
AHIS279

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AARG293

224004

PDB entries from 2024-08-21

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