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2QDY

Crystal Structure of Fe-type NHase from Rhodococcus erythropolis AJ270

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0016829molecular_functionlyase activity
A0018822molecular_functionnitrile hydratase activity
A0046872molecular_functionmetal ion binding
A0046914molecular_functiontransition metal ion binding
B0016829molecular_functionlyase activity
B0018822molecular_functionnitrile hydratase activity
B0046914molecular_functiontransition metal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FE A 300
ChainResidue
ACYS110
ASER114
AHOH2172

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 2001
ChainResidue
BTHR121
BARG132
BLEU208
BHOH2337

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 2002
ChainResidue
BGLU31
BTRP32
ASER20
ATRP24

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 2003
ChainResidue
BGLU134
BTYR135
BSER192
BHOH2182

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 2004
ChainResidue
AGLN174
AARG175
AHOH2191
AHOH2207

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 2005
ChainResidue
BHOH2020
BHOH2059
BHOH2064
BHOH2073
BHOH2091
BHOH2224

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 2006
ChainResidue
AHOH2077
AHOH2162
BHOH2214
BHOH2227
BHOH2252

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 2007
ChainResidue
AHOH2238
BHOH2081
BHOH2314
BHOH2321
BHOH2328

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE IBN B 1000
ChainResidue
AGLN91
AHOH2175
BTYR37
BMET40
BTYR72
BTYR76

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1100
ChainResidue
ATYR40
AGLY43
ATRP44
ATHR47
AHOH2199

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1200
ChainResidue
AASP77
AGLY78
ATHR79
ATYR94
AILE95
AHOH2088
BTHR158

site_idBC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL B 1300
ChainResidue
AARG139
AGLU140
BGLN11
BPRO137
BASP193
BTHR194
BASP195
BHOH2095
BHOH2129
BHOH2170
BHOH2189

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 1400
ChainResidue
BARG147
BGLY148
BARG149
BHOH2089
BHOH2133
BHOH2288

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 1500
ChainResidue
ATYR161
BSER154
BHIS155
BHIS181
BHOH2106
BHOH2199

site_idBC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GOL B 1600
ChainResidue
ATRP65
ATHR66
AASP67
APRO68
AARG175
AHOH2061
BGLN92
BASP93
BHOH2102
BHOH2214
BHOH2227
BHOH2333

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9586994","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2AHJ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"Cysteine sulfinic acid (-SO2H)","evidences":[{"source":"PubMed","id":"9368004","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9586994","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Cysteine sulfenic acid (-SOH)","evidences":[{"source":"PubMed","id":"9586994","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ahj
ChainResidueDetails
BARG56

site_idMCSA1
Number of Residues3
DetailsM-CSA 57
ChainResidueDetails
BARG56electrostatic stabiliser, proton acceptor, proton donor
BTYR72proton acceptor, proton donor
BTYR76increase acidity, increase basicity
AGLY122electrofuge, metal ligand, nucleophile, proton acceptor, proton donor

238582

PDB entries from 2025-07-09

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