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5DVX

Crystal structure of the catalytic-domain of human carbonic anhydrase IX at 1.6 angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004089molecular_functioncarbonate dehydratase activity
A0008270molecular_functionzinc ion binding
B0004089molecular_functioncarbonate dehydratase activity
B0008270molecular_functionzinc ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 401
ChainResidue
AHIS226
AHIS228
AHIS251
AHOH606

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 402
ChainResidue
AHIS140
ATRP141
AHIS200
BHIS244

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL A 403
ChainResidue
AHOH506
AHOH638
AHOH755
AGLN224

site_idAC4
Number of Residues8
Detailsbinding site for residue GOL A 404
ChainResidue
AARG151
AGLN326
ATYR327
AGLU328
AILE341
AHOH512
AHOH538
AHOH595

site_idAC5
Number of Residues8
Detailsbinding site for residue GOL A 405
ChainResidue
AARG151
AVAL152
AGLU387
AHOH521
AHOH646
BGLY393
BVAL394
BASP395

site_idAC6
Number of Residues2
Detailsbinding site for residue CL A 406
ChainResidue
AARG159
AGLN338

site_idAC7
Number of Residues2
Detailsbinding site for residue CL A 407
ChainResidue
AGLU242
AHOH579

site_idAC8
Number of Residues5
Detailsbinding site for residue TRS A 408
ChainResidue
ALEU373
APHE375
AHOH575
AHOH611
AHOH675

site_idAC9
Number of Residues4
Detailsbinding site for residue ZN A 409
ChainResidue
AHIS244
BTRP141
BHIS200
BHOH671

site_idAD1
Number of Residues4
Detailsbinding site for residue ZN B 401
ChainResidue
BHIS226
BHIS228
BHIS251
BHOH575

site_idAD2
Number of Residues6
Detailsbinding site for residue GOL B 402
ChainResidue
BGLN224
BVAL253
BHOH586
BHOH602
BHOH611
BHOH683

site_idAD3
Number of Residues4
Detailsbinding site for residue GOL B 403
ChainResidue
BPRO269
BGLY270
BGLU328
BHOH511

site_idAD4
Number of Residues6
Detailsbinding site for residue GOL B 404
ChainResidue
APRO208
BPHE160
BARG384
BHOH514
BHOH547
BHOH707

site_idAD5
Number of Residues2
Detailsbinding site for residue CL B 405
ChainResidue
BARG159
BGLN338

Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVeghrFpaEIHVV
ChainResidueDetails
ASER237-VAL253

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
AHIS200
BHIS200

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:19805286
ChainResidueDetails
AHIS226
AHIS228
AHIS251
BHIS226
BHIS228
BHIS251

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
ATHR332
BTHR332

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:18703501, ECO:0000269|PubMed:19805286
ChainResidueDetails
AASN346
BASN346

218853

PDB entries from 2024-04-24

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