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4NI2

Crystal structure of the heterodimeric catalytic domain of wild-type human soluble guanylate cyclase

Functional Information from GO Data
ChainGOidnamespacecontents
A0009190biological_processcyclic nucleotide biosynthetic process
A0016849molecular_functionphosphorus-oxygen lyase activity
A0035556biological_processintracellular signal transduction
B0009190biological_processcyclic nucleotide biosynthetic process
B0016849molecular_functionphosphorus-oxygen lyase activity
B0035556biological_processintracellular signal transduction
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 701
ChainResidue
AVAL525
AGLU526
ALEU596
AHOH810
AHOH839

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 702
ChainResidue
AALA531
AHOH812
AHOH868
AASP486
AILE487
ATYR510
AGLY529

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 701
ChainResidue
AILE528
AGLY529
AHOH877
BGLU473
BTHR474
BMET480
BHOH837

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 702
ChainResidue
ALYS590
BPHE468
BGLY484
BLEU485
BPRO486
BGLU487

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 703
ChainResidue
BILE427
BVAL428
BTHR520
BGLU554
BHOH828
BHOH896

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 704
ChainResidue
BVAL428
BGLY429
BHOH812

Functional Information from PROSITE/UniProt
site_idPS00452
Number of Residues24
DetailsGUANYLATE_CYCLASE_1 Guanylate cyclase signature. GVV.GvkmprYcLFGNNVTlankfE
ChainResidueDetails
AGLY585-GLU608
BGLY531-GLU554

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues260
DetailsDomain: {"description":"Guanylate cyclase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00099","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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