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3HMK

Crystal Structure of Serine Racemase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0003941molecular_functionL-serine ammonia-lyase activity
A0005509molecular_functioncalcium ion binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006520biological_processamino acid metabolic process
A0006563biological_processL-serine metabolic process
A0008721molecular_functionD-serine ammonia-lyase activity
A0009069biological_processserine family amino acid metabolic process
A0009410biological_processresponse to xenobiotic stimulus
A0014070biological_processresponse to organic cyclic compound
A0016594molecular_functionglycine binding
A0016829molecular_functionlyase activity
A0016853molecular_functionisomerase activity
A0018114molecular_functionthreonine racemase activity
A0030165molecular_functionPDZ domain binding
A0030170molecular_functionpyridoxal phosphate binding
A0030378molecular_functionserine racemase activity
A0032496biological_processresponse to lipopolysaccharide
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0042866biological_processpyruvate biosynthetic process
A0043025cellular_componentneuronal cell body
A0045177cellular_componentapical part of cell
A0046872molecular_functionmetal ion binding
A0070178biological_processD-serine metabolic process
A0070179biological_processD-serine biosynthetic process
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0003941molecular_functionL-serine ammonia-lyase activity
B0005509molecular_functioncalcium ion binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006520biological_processamino acid metabolic process
B0006563biological_processL-serine metabolic process
B0008721molecular_functionD-serine ammonia-lyase activity
B0009069biological_processserine family amino acid metabolic process
B0009410biological_processresponse to xenobiotic stimulus
B0014070biological_processresponse to organic cyclic compound
B0016594molecular_functionglycine binding
B0016829molecular_functionlyase activity
B0016853molecular_functionisomerase activity
B0018114molecular_functionthreonine racemase activity
B0030165molecular_functionPDZ domain binding
B0030170molecular_functionpyridoxal phosphate binding
B0030378molecular_functionserine racemase activity
B0032496biological_processresponse to lipopolysaccharide
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0042866biological_processpyruvate biosynthetic process
B0043025cellular_componentneuronal cell body
B0045177cellular_componentapical part of cell
B0046872molecular_functionmetal ion binding
B0070178biological_processD-serine metabolic process
B0070179biological_processD-serine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 340
ChainResidue
AGLU210
AALA214
AASP216
AHOH375
AHOH395

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PLP A 350
ChainResidue
AGLY186
AGLY187
AGLY188
AMET189
AGLY239
AVAL240
ATHR285
ASER313
AGLY314
AHOH346
AHOH409
AHOH454
APHE55
ALYS56
AASN86
AGLY185

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 340
ChainResidue
BGLU210
BALA214
BASP216
BHOH351
BHOH361
BHOH394

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PLP B 350
ChainResidue
BPHE55
BLYS56
BASN86
BGLY185
BGLY186
BGLY187
BGLY188
BMET189
BGLY239
BGLU283
BTHR285
BSER313
BHOH421
BHOH424

Functional Information from PROSITE/UniProt
site_idPS00165
Number of Residues14
DetailsDEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. Elfqk.TGSFKIRGA
ChainResidueDetails
AGLU47-ALA60

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
ALYS56
ASER84
BLYS56
BSER84

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASP238
BLYS51
BTYR121
BGLU210
BASP216
BASP238
ALYS51
ATYR121
AGLU210
AASP216

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AARG135
BARG135

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AALA214
BALA214

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
ALYS56
BLYS56

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9QZX7
ChainResidueDetails
ATHR71
BTHR71

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:Q9QZX7
ChainResidueDetails
ACYS113
BCYS113

219869

PDB entries from 2024-05-15

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