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1J0D

ACC deaminase mutant complexed with ACC

Functional Information from GO Data
ChainGOidnamespacecontents
A0008660molecular_function1-aminocyclopropane-1-carboxylate deaminase activity
A0009310biological_processamine catabolic process
A0016787molecular_functionhydrolase activity
A0030170molecular_functionpyridoxal phosphate binding
B0008660molecular_function1-aminocyclopropane-1-carboxylate deaminase activity
B0009310biological_processamine catabolic process
B0016787molecular_functionhydrolase activity
B0030170molecular_functionpyridoxal phosphate binding
C0008660molecular_function1-aminocyclopropane-1-carboxylate deaminase activity
C0009310biological_processamine catabolic process
C0016787molecular_functionhydrolase activity
C0030170molecular_functionpyridoxal phosphate binding
D0008660molecular_function1-aminocyclopropane-1-carboxylate deaminase activity
D0009310biological_processamine catabolic process
D0016787molecular_functionhydrolase activity
D0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE 5PA A 1401
ChainResidue
ALYS54
ASER166
ACYS200
AVAL201
ATHR202
AGLY203
ASER204
ATHR205
ATYR295
AGLU296
AHOH1467
AGLY74
AHOH1477
AGLY75
ASER78
AASN79
AGLN80
ATRP102
AALA163
AGLY164

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE 5PA B 1501
ChainResidue
BASN50
BLYS54
BSER78
BASN79
BGLN80
BGLY164
BCYS200
BVAL201
BTHR202
BGLY203
BSER204
BTHR205
BTYR295
BGLU296
BLEU323
BGLY324
BGLY325
BHOH1507
BHOH1574

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR RESIDUE 5PA C 1601
ChainResidue
CASN50
CLYS54
CSER78
CASN79
CGLN80
CGLY164
CCYS200
CVAL201
CTHR202
CGLY203
CTHR205
CTYR295
CGLU296
CLEU323
CGLY324
CGLY325
CHOH1603
CHOH1611
CHOH1734
CHOH1736

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE 5PA D 1701
ChainResidue
DASN50
DLYS54
DSER78
DASN79
DGLN80
DALA163
DGLY164
DVAL201
DTHR202
DGLY203
DSER204
DTHR205
DTYR295
DGLU296
DLEU323
DGLY324
DGLY325
DHOH1710
DHOH1760
DHOH1820

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Nucleophile
ChainResidueDetails
ASER78
BSER78
CSER78
DSER78

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:9604000
ChainResidueDetails
AALA1
BALA1
CALA1
DALA1

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
ATHR51
BTHR51
CTHR51
DTHR51

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1f2d
ChainResidueDetails
ATHR81
ATHR51
AGLU296
ASER78
ATYR295

site_idCSA10
Number of Residues1
DetailsAnnotated By Reference To The Literature 1f2d
ChainResidueDetails
BTHR51

site_idCSA11
Number of Residues1
DetailsAnnotated By Reference To The Literature 1f2d
ChainResidueDetails
CTHR51

site_idCSA12
Number of Residues1
DetailsAnnotated By Reference To The Literature 1f2d
ChainResidueDetails
DTHR51

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1f2d
ChainResidueDetails
BTHR81
BTHR51
BGLU296
BSER78
BTYR295

site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 1f2d
ChainResidueDetails
CTHR81
CTHR51
CGLU296
CSER78
CTYR295

site_idCSA4
Number of Residues5
DetailsAnnotated By Reference To The Literature 1f2d
ChainResidueDetails
DTHR81
DTHR51
DGLU296
DSER78
DTYR295

site_idCSA5
Number of Residues1
DetailsAnnotated By Reference To The Literature 1f2d
ChainResidueDetails
AGLY48

site_idCSA6
Number of Residues1
DetailsAnnotated By Reference To The Literature 1f2d
ChainResidueDetails
BGLY48

site_idCSA7
Number of Residues1
DetailsAnnotated By Reference To The Literature 1f2d
ChainResidueDetails
CGLY48

site_idCSA8
Number of Residues1
DetailsAnnotated By Reference To The Literature 1f2d
ChainResidueDetails
DGLY48

site_idCSA9
Number of Residues1
DetailsAnnotated By Reference To The Literature 1f2d
ChainResidueDetails
ATHR51

site_idMCSA1
Number of Residues3
DetailsM-CSA 545
ChainResidueDetails
ATHR51covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor
ATYR269covalently attached, electrostatic stabiliser, nucleofuge, nucleophile
ATYR295electrostatic stabiliser, proton acceptor, proton donor

site_idMCSA2
Number of Residues3
DetailsM-CSA 545
ChainResidueDetails
BTHR51covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor
BTYR269covalently attached, electrostatic stabiliser, nucleofuge, nucleophile
BTYR295electrostatic stabiliser, proton acceptor, proton donor

site_idMCSA3
Number of Residues3
DetailsM-CSA 545
ChainResidueDetails
CTHR51covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor
CTYR269covalently attached, electrostatic stabiliser, nucleofuge, nucleophile
CTYR295electrostatic stabiliser, proton acceptor, proton donor

site_idMCSA4
Number of Residues3
DetailsM-CSA 545
ChainResidueDetails
DTHR51covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor
DTYR269covalently attached, electrostatic stabiliser, nucleofuge, nucleophile
DTYR295electrostatic stabiliser, proton acceptor, proton donor

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PDB entries from 2024-07-24

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