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6BPX

Crystal structure of cysteine-bound ferrous form of the matured Cl2-Tyr157 human cysteine dioxygenase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000097biological_processsulfur amino acid biosynthetic process
A0005506molecular_functioniron ion binding
A0005829cellular_componentcytosol
A0006534biological_processcysteine metabolic process
A0006954biological_processinflammatory response
A0007595biological_processlactation
A0008198molecular_functionferrous iron binding
A0008270molecular_functionzinc ion binding
A0010243biological_processresponse to organonitrogen compound
A0016151molecular_functionnickel cation binding
A0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
A0017172molecular_functioncysteine dioxygenase activity
A0019448biological_processL-cysteine catabolic process
A0033762biological_processresponse to glucagon
A0042412biological_processtaurine biosynthetic process
A0043200biological_processresponse to amino acid
A0045471biological_processresponse to ethanol
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
A0051384biological_processresponse to glucocorticoid
A0051591biological_processresponse to cAMP
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue FE2 A 301
ChainResidue
AHIS86
AHIS88
AHIS140
ACYS302
AHOH413

site_idAC2
Number of Residues8
Detailsbinding site for residue CYS A 302
ChainResidue
AHIS88
AHIS140
A2LT157
AFE2301
ATYR58
AARG60
ALEU75
AHIS86

site_idAC3
Number of Residues6
Detailsbinding site for residue SO4 A 303
ChainResidue
AGLN34
AARG123
AALA131
ATYR132
AHOH402
AHOH405

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 A 304
ChainResidue
ATYR56
AHIS173
ALYS174
AHOH451

site_idAC5
Number of Residues3
Detailsbinding site for residue SO4 A 305
ChainResidue
ALYS119
AARG141
AGLN169

site_idAC6
Number of Residues3
Detailsbinding site for residue GOL A 306
ChainResidue
AASP168
AHIS173
AASN175

site_idAC7
Number of Residues3
Detailsbinding site for residue GOL A 307
ChainResidue
ATYR58
ASER84
AHOH410

site_idAC8
Number of Residues5
Detailsbinding site for residue GOL A 308
ChainResidue
AALA48
AALA51
AASN90
AHOH433
AHOH440

site_idAC9
Number of Residues8
Detailsbinding site for residue GOL A 309
ChainResidue
APHE53
AASP54
AGLN55
AGLY78
AGLU79
AHIS81
ATRP109
AASP135

site_idAD1
Number of Residues2
Detailsbinding site for residue GOL A 310
ChainResidue
ALEU98
AGLN99

site_idAD2
Number of Residues5
Detailsbinding site for residue GOL A 311
ChainResidue
AARG57
AHIS182
AARG188
APRO190
AASN191

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:17135237
ChainResidueDetails
AHIS86
AHIS88
AHIS140

site_idSWS_FT_FI2
Number of Residues2
DetailsCROSSLNK: 3'-(S-cysteinyl)-tyrosine (Cys-Tyr) => ECO:0000269|PubMed:17135237
ChainResidueDetails
ACYS93
A2LT157

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PDB entries from 2024-06-12

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