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1KMK

E. coli NifS/CsdB protein at 2.20A with the cysteine perselenide intermediate (residue CSZ).

Functional Information from GO Data
ChainGOidnamespacecontents
A0001887biological_processselenium compound metabolic process
A0003824molecular_functioncatalytic activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0006534biological_processcysteine metabolic process
A0006790biological_processsulfur compound metabolic process
A0008826molecular_functioncysteine sulfinate desulfinase activity
A0009000molecular_functionselenocysteine lyase activity
A0016226biological_processiron-sulfur cluster assembly
A0016740molecular_functiontransferase activity
A0016787molecular_functionhydrolase activity
A0016829molecular_functionlyase activity
A0030170molecular_functionpyridoxal phosphate binding
A0031071molecular_functioncysteine desulfurase activity
A0042803molecular_functionprotein homodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SEC A 502
ChainResidue
AALA30
AHOH732
AHIS123
AASN175
AGLN203
ALYS226
AARG359
AARG379
APLP500
AHOH601

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PLP A 500
ChainResidue
ATHR94
ATHR95
AHIS123
AALA125
AASN175
AASP200
AALA202
AGLN203
ASER223
AHIS225
ALYS226
AGLY277
ATHR278
ASEC502
AHOH582
AHOH601

Functional Information from PROSITE/UniProt
site_idPS00595
Number of Residues20
DetailsAA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. CDFYvfSGHKlygpt.GiGiL
ChainResidueDetails
ACYS217-LEU236

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Cysteine persulfide intermediate
ChainResidueDetails
ACSZ364

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
ALYS226

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ecx
ChainResidueDetails
AALA63

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ecx
ChainResidueDetails
ALYS226
AASP200
AHIS124

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ecx
ChainResidueDetails
ALYS226
AASP200
AHIS123

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ecx
ChainResidueDetails
ALYS226

site_idMCSA1
Number of Residues5
DetailsM-CSA 855
ChainResidueDetails
AHIS123increase basicity, proton acceptor, proton donor
AASP200electrostatic stabiliser, polar interaction
AGLN203electrostatic stabiliser, polar interaction
ALYS226covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor
ACSZ364covalently attached, nucleophile, proton donor

222415

PDB entries from 2024-07-10

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