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3FQ8

M248I mutant of GSAM

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0006782biological_processprotoporphyrinogen IX biosynthetic process
A0008483molecular_functiontransaminase activity
A0015995biological_processchlorophyll biosynthetic process
A0016853molecular_functionisomerase activity
A0030170molecular_functionpyridoxal phosphate binding
A0033014biological_processtetrapyrrole biosynthetic process
A0042286molecular_functionglutamate-1-semialdehyde 2,1-aminomutase activity
B0005737cellular_componentcytoplasm
B0006782biological_processprotoporphyrinogen IX biosynthetic process
B0008483molecular_functiontransaminase activity
B0015995biological_processchlorophyll biosynthetic process
B0016853molecular_functionisomerase activity
B0030170molecular_functionpyridoxal phosphate binding
B0033014biological_processtetrapyrrole biosynthetic process
B0042286molecular_functionglutamate-1-semialdehyde 2,1-aminomutase activity
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PMP A5000
ChainResidue
ASER1122
ALYS1273
AHOH7032
AHOH7035
AHOH7037
BGLY2304
BTHR2305
BHOH7036
AGLY1123
ATHR1124
ATYR1150
AGLU1212
AASN1217
AASP1245
AVAL1247
AILE1248

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PMP B6000
ChainResidue
AGLY1304
ATHR1305
AHOH7080
BSER2122
BGLY2123
BTHR2124
BTYR2150
BGLU2212
BASN2217
BASP2245
BVAL2247
BILE2248
BLYS2273
BHOH7079
BHOH7612

Functional Information from PROSITE/UniProt
site_idPS00600
Number of Residues37
DetailsAA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LVfDEVit.GF.RiAyggvqekfgvtp....DLTtlGKiigGG
ChainResidueDetails
ALEU1242-GLY1278

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
ALYS1273
BLYS2273

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1b8g
ChainResidueDetails
AASP1245
ALYS1273
ATYR1150

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1b8g
ChainResidueDetails
BLYS2273
BTYR2150
BASP2245

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1b8g
ChainResidueDetails
AASP1245
ATYR1150

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1b8g
ChainResidueDetails
BTYR2150
BASP2245

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1b8g
ChainResidueDetails
APHE1157
AASP1245
ALYS1273

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1b8g
ChainResidueDetails
BLYS2273
BPHE2157
BASP2245

site_idMCSA1
Number of Residues3
DetailsM-CSA 195
ChainResidueDetails
ATYR1150steric role
AASP1245electrostatic stabiliser, hydrogen bond acceptor
ALYS1273covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor

site_idMCSA2
Number of Residues3
DetailsM-CSA 195
ChainResidueDetails
BTYR2150steric role
BASP2245electrostatic stabiliser, hydrogen bond acceptor
BLYS2273covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor

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PDB entries from 2024-07-31

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