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2E7U

Crystal structure of glutamate-1-semialdehyde 2,1-aminomutase from Thermus thermophilus HB8

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0006779biological_processporphyrin-containing compound biosynthetic process
A0006782biological_processprotoporphyrinogen IX biosynthetic process
A0008483molecular_functiontransaminase activity
A0016853molecular_functionisomerase activity
A0030170molecular_functionpyridoxal phosphate binding
A0033014biological_processtetrapyrrole biosynthetic process
A0042286molecular_functionglutamate-1-semialdehyde 2,1-aminomutase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 1002
ChainResidue
AASN211
APHE399
AGLU400
AHOH1068
AHOH1230

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 1003
ChainResidue
AHOH1078
AHOH1210
AGLY156
AGLY158
ALEU160
AHOH1053

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PMP A 1001
ChainResidue
ASER116
AGLY117
ATHR118
ATYR144
AHIS145
AASN211
AASP238
AVAL240
AMET241
AGLY297
ATHR298
AHOH1071

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 1004
ChainResidue
AARG103
AALA104
AGLU253
AHOH1214

Functional Information from PROSITE/UniProt
site_idPS00600
Number of Residues37
DetailsAA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIaDEVmt.GF.RlAfggatellglkp....DLVtlGKilgGG
ChainResidueDetails
ALEU235-GLY271

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_00375
ChainResidueDetails
ALYS266

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1b8g
ChainResidueDetails
AASP238
ATYR144

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1b8g
ChainResidueDetails
ALYS266
AASP238
ATYR144

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PDB entries from 2024-07-24

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