eF-site ID 1boa-A PDB Code 1boa Chain A click to enlarge Title HUMAN METHIONINE AMINOPEPTIDASE 2 COMPLEXED WITH ANGIOGENESIS INHIBITOR FUMAGILLIN Classification AMINOPEPTIDASE Compound METHIONINE AMINOPEPTIDASE Source Homo sapiens (Human) (AMPM2_HUMAN) Sequence A:  KVQTDPPSVPICDLYPNGVFPKGQECEYPEKKALDQASEE IWNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCS RKLIKENGLNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQY DDICKIDFGTHISGRIIDCAFTVTFNPKYDTLLKAVKDAT NTGIKCAGIDVRLCDVGEAIQEVMESYEVEIDGKTYQVKP IRNLNGHSIGQYRIHAGKTVPIIKGGEATRMEEGEVYAIE TFGSTGKGVVHDDMECSHYMKNFDVGHVPIRLPRTKHLLN VINENFGTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPY PPLCDIKGSYTAQFEHTILLRPTCKEVVSRGDDY Description Functional site 1) chain A residue 251 type sequence D description DICOBALT ACTIVE SITE source : CO2 2) chain A residue 262 type sequence D description DICOBALT ACTIVE SITE source : CO2 3) chain A residue 459 type sequence E description DICOBALT ACTIVE SITE source : CO2 4) chain A residue 331 type sequence H description DICOBALT ACTIVE SITE source : CO2 5) chain A residue 364 type sequence E description DICOBALT ACTIVE SITE source : CO2 6) chain A residue 231 type sequence H description FUMAGILLIN 480 FORMS A COVALENT BOND WITH HIS 231 source : BND 7) chain A residue 262 type sequence D description BINDING SITE FOR RESIDUE CO A 481 source : AC1 8) chain A residue 331 type sequence H description BINDING SITE FOR RESIDUE CO A 481 source : AC1 9) chain A residue 364 type sequence E description BINDING SITE FOR RESIDUE CO A 481 source : AC1 10) chain A residue 459 type sequence E description BINDING SITE FOR RESIDUE CO A 481 source : AC1 11) chain A residue 251 type sequence D description BINDING SITE FOR RESIDUE CO A 482 source : AC2 12) chain A residue 262 type sequence D description BINDING SITE FOR RESIDUE CO A 482 source : AC2 13) chain A residue 459 type sequence E description BINDING SITE FOR RESIDUE CO A 482 source : AC2 14) chain A residue 231 type sequence H description BINDING SITE FOR RESIDUE FUG A 480 source : AC3 15) chain A residue 327 type sequence N description BINDING SITE FOR RESIDUE FUG A 480 source : AC3 16) chain A residue 328 type sequence L description BINDING SITE FOR RESIDUE FUG A 480 source : AC3 17) chain A residue 329 type sequence N description BINDING SITE FOR RESIDUE FUG A 480 source : AC3 18) chain A residue 331 type sequence H description BINDING SITE FOR RESIDUE FUG A 480 source : AC3 19) chain A residue 339 type sequence H description BINDING SITE FOR RESIDUE FUG A 480 source : AC3 20) chain A residue 364 type sequence E description BINDING SITE FOR RESIDUE FUG A 480 source : AC3 21) chain A residue 375 type sequence H description BINDING SITE FOR RESIDUE FUG A 480 source : AC3 22) chain A residue 376 type sequence D description BINDING SITE FOR RESIDUE FUG A 480 source : AC3 23) chain A residue 444 type sequence Y description BINDING SITE FOR RESIDUE FUG A 480 source : AC3 24) chain A residue 231 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:16540317 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 339 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:16540317 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 251 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:14534293, ECO:0000269|PubMed:16134930, ECO:0000269|PubMed:16540317, ECO:0000269|PubMed:17350258, ECO:0000269|PubMed:17636946 source Swiss-Prot : SWS_FT_FI2 27) chain A residue 262 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:14534293, ECO:0000269|PubMed:16134930, ECO:0000269|PubMed:16540317, ECO:0000269|PubMed:17350258, ECO:0000269|PubMed:17636946 source Swiss-Prot : SWS_FT_FI2 28) chain A residue 331 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:14534293, ECO:0000269|PubMed:16134930, ECO:0000269|PubMed:16540317, ECO:0000269|PubMed:17350258, ECO:0000269|PubMed:17636946 source Swiss-Prot : SWS_FT_FI2 29) chain A residue 364 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:14534293, ECO:0000269|PubMed:16134930, ECO:0000269|PubMed:16540317, ECO:0000269|PubMed:17350258, ECO:0000269|PubMed:17636946 source Swiss-Prot : SWS_FT_FI2 30) chain A residue 459 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:14534293, ECO:0000269|PubMed:16134930, ECO:0000269|PubMed:16540317, ECO:0000269|PubMed:17350258, ECO:0000269|PubMed:17636946 source Swiss-Prot : SWS_FT_FI2 31) chain A residue 246-262 type prosite sequence DICKIDFGTHISGRIID description MAP_2 Methionine aminopeptidase subfamily 2 signature. DIcKIDfGtHISGriiD source prosite : PS01202

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