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1XRS

Crystal structure of Lysine 5,6-Aminomutase in complex with PLP, cobalamin, and 5'-deoxyadenosine

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0016853molecular_functionisomerase activity
A0031419molecular_functioncobalamin binding
A0047826molecular_functionD-lysine 5,6-aminomutase activity
B0016853molecular_functionisomerase activity
B0031419molecular_functioncobalamin binding
B0046872molecular_functionmetal ion binding
B0046983molecular_functionprotein dimerization activity
B0047826molecular_functionD-lysine 5,6-aminomutase activity
Functional Information from PDB Data
site_idAC1
Number of Residues27
DetailsBINDING SITE FOR RESIDUE B12 B 800
ChainResidue
ALYS516
BTYR146
BLEU185
BVAL186
BSER187
BVAL190
BTHR191
BGLN192
BLEU219
BGLY221
BGLY222
BTHR130
BPRO223
BPHE239
BGLY240
BPRO241
BARG243
BPHE244
BVAL248
B5AD500
BASP131
BALA132
BHIS133
BTHR134
BVAL135
BGLY136
BILE140

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PLP B 801
ChainResidue
AARG184
ATHR186
AGLY187
AGLN188
ASER189
ATYR236
ASER238
ATYR263
AARG268
AASN299
BLYS144

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE 5AD B 500
ChainResidue
AASP54
AGLU55
AVAL56
ATYR193
BB12800

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15514022
ChainResidueDetails
BTHR130
BLEU185
BLEU219
BPHE239
AASN271
ATHR302

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000312|PDB:1XRS
ChainResidueDetails
BHIS133

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:15514022
ChainResidueDetails
BLYS144

Catalytic Information from CSA
site_idCSA1
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 13679082
ChainResidueDetails
BLYS144

site_idMCSA1
Number of Residues1
DetailsM-CSA 737
ChainResidueDetails
BLYS144electron pair acceptor, electron pair donor, nucleofuge, nucleophile
ALEU301promote homolysis
APRO373promote homolysis

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PDB entries from 2024-09-04

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